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

dc.contributor.advisor Lenny, James
dc.contributor.author Chang, Melvin
dc.contributor.department Biology
dc.date.accessioned 2014-01-15T20:05:35Z
dc.date.available 2014-01-15T20:05:35Z
dc.date.issued 2014-01-15
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.
dc.format.extent viii, 47 pages
dc.identifier.uri http://hdl.handle.net/10125/32008
dc.publisher University of Hawaii at Manoa
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.
dc.title The Isolation And Characterization Of A Yeast Protein Which Specifically Inhibits Yeast Proteinase A
dc.type Term Project
dc.type.dcmi Text
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