Primary structure of the activation segment of procarboxypeptidase a from porcine pancreas

J. Vendrell, F. X. Avilés, E. Genescá, B. San Segundo, F. Soriano, E. Méndez

Research output: Contribution to journalArticleResearchpeer-review

15 Citations (Scopus)

Abstract

The complete primary structure of the activation segment of monomeric procarboxypeptidase A from porcine pancreas has been determined by automated and manual Edman-like degradation methods performed on its fragments generated by enzymatic cleavage. The polypeptide consists of 94 residues, with a molecular mass of 10, 768, and presents a high proportion of acidic and hydrophobic residues and a proline-rich region in the center of the molecule. Comparison of this sequence with the already reported equivalent sequence deduced from rat procarboxypeptidase A cDNA reveals a very high degree of homology between the two propeptides (up to a 81% of identities), which is even higher in certain large zones of the molecule. © 1986 Academic Press, Inc.
Original languageEnglish
Pages (from-to)517-523
JournalBiochemical and Biophysical Research Communications
Volume141
DOIs
Publication statusPublished - 15 Dec 1986

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