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Sequential Homologies Between Procarboxypeptidases A and B From Porcine Pancreas

Sequential Homologies Between Procarboxypeptidases A and B From Porcine Pancreas

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

Biochem Biophys Res Commun. 1985 Jul 16;130(1):97-103.

PMID: 4026847

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 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9025245-C	Carboxypeptidase B from porcine pancreas		9025-24-5	Price

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