INVESTIGADORES
SEQUEIROS Cynthia
artículos
Título:
Comparison of Two Cysteine Endopeptidases from Pseudananas macrodontes (Morr.) Harms (Bromeliaceae)
Autor/es:
L.M.I. LóPEZ, C. SEQUEIROS, S.A. TREJO, M. F. PARDO, N. O. CAFFINI AND C. L. NATALUCCI
Revista:
BIOLOGICAL CHEMISTRY
Editorial:
Walter de Gruyter
Referencias:
Lugar: Berlin; Año: 2001 vol. 382 p. 875 - 878
ISSN:
1431-6730
Resumen:
The properties of two cysteine peptidases (macrodontain I and II) isolated from fruits of Pseudananas macrodontes have been compared. The enzymes showed optimum pH ranges near neutrality and were inhibited by E-64 and other cysteine peptidase inhibitors. Molecular masses were 23459 and 23703 kDa, the isoelectric points were 6.1 and 5.9, and the K values were 13.4 and 8.9 M (Bz-Phe-Val-Arg-AMC) for macrodontain I and II, respectively. N-á-CBZ-L-amino acid p-nitrophenyl esters were tested for both enzymes. The Nterminal sequences of both proteases differed slightly and showed high sequence similarity to other pineapple stem-derived cysteine endopeptidases.