Isolation and Characterization of the Carboxypeptidase Y Inhibitor from Yeast

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 Se...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1974-12, Vol.71 (12), p.4874-4878
Main Authors: Matern, Heidrun, Hoffmann, Marion, Holzer, Helmut
Format: Article
Language:English
Subjects:
Acetone
Biological Sciences: Biochemistry
Carboxypeptidases - antagonists & inhibitors
Chemical Precipitation
Chromatography
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis
Electrophoresis, Disc
Enzyme Inhibitors - antagonists & inhibitors
Enzyme Inhibitors - isolation & purification
Filtration
Fractionation
Gels
Hydroxyapatites
Molecular Weight
Pancreas
Peptide Hydrolases - pharmacology
Potassium phosphates
Protamines
Saccharomyces cerevisiae - analysis
Solvents
Sulfates
Ungulates
Yeasts
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.71.12.4874