Porcine carboxypeptidase B. I. Affinity chromatography and specificity

Mordechai Sokolovsky, Nava Zisapel

Research output: Contribution to journalArticlepeer-review

Abstract

Porcine carboxypeptidase B (peptidyl-l-lysine hydrolase, EC 3.4.2.2), was found to possess in addition to its known specificity toward basic substrates an intrinsic activity with specificity similar to that of carboxypeptidase A (peptidyl-l-amino acid hydrolase, EC 3.4.2.1). Affinity chromatography using a water insoluble derivative of the inhibitor d-Ala-l-Arg was employed in order to establish that the activities toward non-basic substrates are intrinsic and not due to contamination present in the commercial porcine carboxypeptidaes B.

Original languageEnglish
Pages (from-to)203-206
Number of pages4
JournalBBA - Enzymology
Volume250
Issue number1
DOIs
StatePublished - 20 Oct 1971

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