Isolation and properties of two inhibitors of proteinase B from yeast.

Abstract In continuation of our studies on the inactivation of tryptophan synthase from Saccharomyces cerevisiae by proteinases from the same organism, two protein inhibitors of the tryptophan synthase inactivating yeast proteinase B were purified from boiled bakers' yeast extract. The molecular weight of both inhibitors is 10,000 and both inhibit specifically proteinase B, but not proteinases A and C. The inhibitors form tight complexes with proteinase B. With the substrates Azocoll and N-acetyltyrosine ethyl ester, noncompetitive inhibition patterns are obtained. The inhibitors are proteins with isoelectric points of 8.0 and 7.0, respectively. They are very stable in the pH range of 1 to 10, but they are easily destroyed by incubation with proteinase A and, less effectively, with proteinase B at pH 5.0. A close molecular relationship of both inhibitors is indicated by the cross-reaction of inhibitor I with antiserum prepared against inhibitor II.

• Publication year

  1974

• Venue

  Journal of Biological Chemistry

• Publication date

  1974-07-25

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(19)42449-6PMID 4210507
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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