Neutral and acid proteinases from free living nematode Turbatrix aceti. Partial purification and characterization

A. Gertler*, Z. Madar, Y. Haas

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

1. 1. Neutral and acid proteinases from Turbatrix aceti were isolated and partially purified, 400-500-fold and characterized. 2. 2. Neutral proteinase is a thiol proteinase with a molecular weight of 22000 and pH optimum of 6.5. It exhibits chymotrypsin-like specificity and is inhibited by p-mercuribenzoate and β-mercaptoethanol. 3. 3. Neutral proteinase is also inhibited by a specific irreversible inhibitor of serine proteinases-diisopropylphosphofluoridate with second-order rate constant of inactivation = 21 min-1 M-1. However, it is not effected by high molecular weight inhibitors of serine proteinases. 4. 4. Acid proteinase is a typical carboxyl proteinase with a molecular weight of 60,000 and pH optimum of 3.5. It is inhibited by a specific inhibitor of carboxyl proteinases 1,2-epoxy-3-(p-nitrophenoxy) propane.

Original languageEnglish
Pages (from-to)357-362
Number of pages6
JournalComparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
Volume64
Issue number4
DOIs
StatePublished - 1979

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