CIHIDECAR   12529
CENTRO DE INVESTIGACIONES EN HIDRATOS DE CARBONO
Unidad Ejecutora - UE
artículos
Título:
Novel cysteine proteinase in Trypanosoma cruzi metacyclogenesis
Autor/es:
DUSCHAK,VILMA G.,; BARBOZA, MARIANA,; GARCIA, G.A.,; LAMMEL, ESTELA M.,; COUTO ALICIA. S.; ISOLA ESTELA L. D.
Revista:
PARASITOLOGY
Editorial:
Cambridge University Press-
Referencias:
Lugar: London; Año: 2006 vol. 132 p. 345 - 355
ISSN:
0031-1820
Resumen:
With the aim to study proteinases released to the culture medium during Trypanosoma cruzi metacyclogenesis, the presence
of cysteine proteinases (CPs) was analysed in culture supernatants obtained throughout the differentiation induced by
stimulation of epimastigotes with Triatoma infestans hindgut homogenate. In SDS-gelatin containing gels, an important
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
of cysteine proteinases (CPs) was analysed in culture supernatants obtained throughout the differentiation induced by
stimulation of epimastigotes with Triatoma infestans hindgut homogenate. In SDS-gelatin containing gels, an important
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
of cysteine proteinases (CPs) was analysed in culture supernatants obtained throughout the differentiation induced by
stimulation of epimastigotes with Triatoma infestans hindgut homogenate. In SDS-gelatin containing gels, an important
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
Trypanosoma cruzi metacyclogenesis, the presence
of cysteine proteinases (CPs) was analysed in culture supernatants obtained throughout the differentiation induced by
stimulation of epimastigotes with Triatoma infestans hindgut homogenate. In SDS-gelatin containing gels, an important
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or
PMSF. This novel CP, named TcCPmet, showed affinity to cystatin-Sepharose, denoting its thiol-proteinase character
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
as well as to ConA-Sepharose, indicating it contains N-linked oligosaccharides. However, it presented a different elution
pattern on ConA-Sepharose than cruzipain and, in addition, it was not recognized by anti-cruzipain serum, facts that
strongly suggest the different nature of both CPs. Moroever, evidence is presented indicating that TcCPmet was able to
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
hydrolyse the same chromogenic peptides as cruzipain at optimal alkaline pH values, although with a different order of
effectiveness. Our results indicate the presence of a novel CP secreted by metacyclic trypomastigotes and reinforces the
important role of these enzymes in metacyclogenesis.
Triatoma infestans hindgut homogenate. In SDS-gelatin containing gels, an important
endopeptidase activity with apparent molecular weight range between 97 and 116 kDa was encountered at pH 6, which
was abolished by the specific cysteine proteinase inhibitor E-64 and TLCK, but not by pepstatin, 1,10 phenantroline or