Pressure and protein denaturation
- Creators
- Johnson, Frank H.
- Campbell, Dan H.
Abstract
Kinetic analyses have indicated that moderate hydrostatic pressures, up to some 700 atmospheres, oppose reversible and irreversible denaturations of certain enzyme systems, apparent at temperatures above the normal optimum of the enzyme reaction, as well as at lower temperatures in the presence of denaturants such as alcohol (1-4). Qualitative observations have shown that such pressures also retard the precipitation of highly purified human serum globulin and egg albumin at 65° (5) and slow the destruction of specific antitoxic activity at the same temperature (6). In this study we have obtained quantitative data with regard to the influence of various pressures, up to 10,000 pounds per sq. in., and of low concentrations of ethyl alcohol on the time course of precipitation of human serum globulin (1) at 65° and pH 6.0.
Additional Information
© 1946 American Society of Biological Chemists. Received for publication, February 6, 1946. The authors take pleasure in acknowledging the interest as well as lengthy discussions and assistance of Professor Linus Pauling in connection with this study. [F.H.J. was a] Fellow of the John Simon Guggenheim Memorial Foundation, from the Department of Biology, Princeton University, Princeton, New Jersey.Attached Files
Published - JOHjbc46.pdf
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Additional details
- Eprint ID
- 12080
- Resolver ID
- CaltechAUTHORS:JOHjbc46
- John Simon Guggenheim Foundation
- Created
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2008-10-27Created from EPrint's datestamp field
- Updated
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2019-10-03Created from EPrint's last_modified field