Sequential homologies between procarboxypeptidases A and B from porcine pancreas

F. X. Avilés, J. Vendrell, F. J. Burgos, F. Soriano, E. Méndez

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24 Citations (Web of Science)

Abstract

Automated Edman degradation of monomeric procarboxypeptidases A and B from porcine pancreas shows that their N-terminal regions (from residue 1 to 34-37) present a high degree of sequential homology to each other as well as to other related procarboxypeptidases. Conformational predictions based on these sequences confirm their structural homology and indicate the probable existence of two β-turns, one β-chain and a long α-helix in them. On the other hand, tryptic peptide maps on a reverse-phase column indicate great sequential similarities (if not identity) between monomeric procarboxypeptidase A and the procarboxypeptidase A subunit isolated from its binary complex with proproteinase E. © 1985.
Original languageEnglish
Pages (from-to)97-103
JournalBiochemical and Biophysical Research Communications
Volume130
Issue number1
DOIs
Publication statusPublished - 16 Jul 1985

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