Sequential homologies between procarboxypeptidases A and B from porcine pancreas.
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 beta-turns, one beta-chain and a long alpha-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.
D000595:Amino Acid Sequence; D000818:Animals; D043424:Carboxypeptidase B; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D004792:Enzyme Precursors; D046911:Macromolecular Substances; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D011487:Protein Conformation; D013552:Swine
D004792:Enzyme Precursors; D046911:Macromolecular Substances; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D043424:Carboxypeptidase B