The Isolation And Characterization Of A Yeast Protein Which Specifically Inhibits Yeast Proteinase A

dc.contributor.advisor Lenny, James en_US Chang, Melvin en_US
dc.contributor.department Biology en_US 2014-01-15T20:05:35Z 2014-01-15T20:05:35Z 2014-01-15 en_US
dc.description.abstract A yeast protein was discovered which specifically inhibits proteinase A of Saccharomyces cerevisiae. The inhibitor was purified 8.4-fold using boiling, dialysis and DEAE-cellulose ion-exchange chromatographic steps. The inhibitor, IA, was found to be an unusually thermostable, nondialyzable protein which was not precipitable with trichloroacetic acid, and which adsorbed to DEAE-cellulose at pH 9-10, and CM-Sephadex at pH 6.0. Elution of the inhibitor from DEAE – cellulose was accomplished with 0.01 M Borax buffer, pH 9.1, containing 0.05 M NaCl. Sephadex G-75 gel-filtration and SDS molecular weight disc electrophoresis suggest a molecular weight of about 13,000 for IA. Digestion by trypsin, chymotrypsin, pepsin, subtilisin and yeast carboxypeptidase demonstrated the inhibitor to be of protein nature. IA was found in the greatest concentration in the cytosol of the cell. Possible digestion of IA at pH 2.5 by proteinase A was observed. Digestion of the inhibitor by yeast proteases at pH 6.8 was clearly demonstrated. Lenney's report (6) of proteinase A activation in pH 5.0, yeast autolysates was also confirmed. en_US
dc.format.extent viii, 47 pages en_US
dc.publisher University of Hawaii at Manoa en_US
dc.rights All UHM Honors Projects are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission from the copyright owner. en_US
dc.title The Isolation And Characterization Of A Yeast Protein Which Specifically Inhibits Yeast Proteinase A en_US
dc.type Term Project en_US
dc.type.dcmi Text en_US
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