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. 1974 Dec;71(12):4874–4878. doi: 10.1073/pnas.71.12.4874

Isolation and Characterization of the Carboxypeptidase Y Inhibitor from Yeast

Heidrun Matern 1,2, Marion Hoffmann 1,2, Helmut Holzer 1,2
PMCID: PMC434001  PMID: 4612529

Abstract

Rapid acetone fractionation of crude yeast extract at low temperature separates carboxypeptidase Y inhibitor from the carboxypeptidase Y-inhibitor complex. On a protein basis the inhibitor has been purified 890-fold, resulting in homogeneity as determined by disc electrophoresis and filtration on Sephadex G-75. The molecular weight was calculated to be about 25,000. The inhibitor is heat-labile in crude extracts, whereas in the purified form it loses only 11% of its activity when it is heated at 100° for 5 min. The inhibitor is inactivated by the yeast proteinases A (EC 3.4.23.8) and B (EC 3.4.22.9), respectively, but not by carboxypeptidase Y (EC 3.4.12.8). The inhibitor inhibits carboxypeptidase Y at a 1.5:1.0 protein-based weight ratio by 80%. At the same concentration ratios, proteinases A and B from yeast, as well as bovine pancreas carboxypeptidases A and B, are not inhibited.

Keywords: proteinase inhibitor

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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