Isolation of highly active papaya peptidases A and B from commercial chymopapain

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Four enzyme fractions were isolated from commercial chymopapain (EC 3.4.22.6) by chromatography on carboxymethyl cellulose CM-32 and were further purified on an agarose-mercurial column. Two fractions proved to be different forms of chymopapain B, the other two were papaya peptidase A and papaya peptidase B. The two latter enzymes were examined in detail. In contrast to previous findings, papaya peptidases exhibited high specific activity, similar to that of papain, (EC 3.4.22.2) and contained about 1 mol -SH group per mol enzyme. These results are not consistent with the idea that the essential -SH group of papaya peptidase A is 'masked' in the native state, but rather suggest that previous preparations contained a substantial amount of inactive enzyme.

Original languageEnglish
Pages (from-to)262-269
Number of pages8
JournalBBA - Enzymology
Volume658
Issue number2
DOIs
Publication statusPublished - Apr 14 1981

Fingerprint

glycyl endopeptidase
caricain
Chymopapain
Papain
Enzymes
Carica
Carboxymethylcellulose Sodium
Sepharose
Chromatography
Peptide Hydrolases

Keywords

  • Affinity chromatography
  • Chymopapain
  • Papain
  • Papaya peptidase

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Isolation of highly active papaya peptidases A and B from commercial chymopapain. / Polgár, L.

In: BBA - Enzymology, Vol. 658, No. 2, 14.04.1981, p. 262-269.

Research output: Contribution to journalArticle

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