文章基本信息

标题：Isolation and Characterization of the Carboxypeptidase Y Inhibitor from Yeast
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作者：Heidrun Matern ; Marion Hoffmann ; Helmut Holzer 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：12
页码：4874-4878
DOI：10.1073/pnas.71.12.4874
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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{degrees} 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.
关键词：proteinase inhibitor