INVESTIGADORES
MORCELLE DEL VALLE Susana Raquel
artículos
Título:
Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
Autor/es:
OBREGÓN, W.D.; ARRIBÉRE, M.C.; MORCELLE DEL VALLE, SUSANA RAQUEL; LIGGIERI, C.; CAFFINI, N. O.; PRIOLO, N. S.
Revista:
JOURNAL OF PROTEIN CHEMISTRY
Editorial:
SPRINGER
Referencias:
Año: 2001 vol. 20 p. 317 - 325
ISSN:
0277-8033
Resumen:
Two new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively. The isoelectric point of araujiain h II was 8.9, whereas araujiain h III had a pI higher than 9.3. Maximum proteolytic activity on caseine was reached at pH 8.0-9.0 for both endopeptidases, which were irreversibly inhibited by iodoacetate and E-64, suggesting they belong to the cysteine protease family. Esterolytic activity was determined on N-alpha-CBZ-amino acid-p-nitrophenyl esters, and the highest kcat/Km values for the both enzymes were obtained with the glutamine derivative. The N-terminal sequences of araujiain h II and araujiain h III showed a high degree of homology with other plant cysteine endopeptidases.
