HOLLNEUGEBAUER, B and RUDOLPH, R and SCHMIDT, M and BUCHNER, J (1991) RECONSTITUTION OF A HEAT-SHOCK EFFECT INVITRO - INFLUENCE OF GROE ON THE THERMAL AGGREGATION OF ALPHA-GLUCOSIDASE FROM YEAST. BIOCHEMISTRY, 30 (50). pp. 11609-11614. ISSN 0006-2960,
Full text not available from this repository.Abstract
Alpha-glucosidase from yeast is inactivated rapidly at temperatures above 42-degrees-C. The thermal inactivation is accompanied by aggregation. The molecular chaperone GroEL suppresses the formation of aggregates by binding the thermally inactivated alpha-glucosidase. Spectroscopic studies suggest that GroEL binds alpha-glucosidase in an intermediately folded state. The complex between alpha-glucosidase and GroEL can be dissolved by MgATP. GroES accelerates the MgATP-dependent dissociation of the alpha-glucosidase-GroEL complex. At elevated temperatures this release leads to the formation of aggregates, while at lower temperatures native, enzymatically active molecules are formed.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RIBULOSE BISPHOSPHATE CARBOXYLASE; ESCHERICHIA-COLI; GENE-PRODUCTS; PROTEINS; PURIFICATION; GROWTH; TEMPERATURES; ATP; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54760 |
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