KERN, G and SCHMIDT, M and BUCHNER, J and JAENICKE, R (1992) GLYCOSYLATION INHIBITS THE INTERACTION OF INVERTASE WITH THE CHAPERONE GROEL. FEBS LETTERS, 305 (3). pp. 203-205. ISSN 0014-5793,
Full text not available from this repository.Abstract
During refolding and reassociation of chemically denatured non-glycosylated invertase froin Saccharomyces cerevisiae, aggregation competes with correct folding, leading to low yields of reactivation (Kern el al. (1992) Protein Sci. 1, 120 131). In the presence of the chaperone GroEL, refolding is completely arrested. This suggests the formation of a stable complex between GroEL and non-native non-glycosylated invertase. Addition of MgATP results in a slow release of active invertase from the chaperone complex. When GroEL/ES and MgATP are present during refolding, the final reactivation yield increases from 14% to 36%. In contrast, refolding of the core-glycosylated and the high-mannose glycosylated forms of invertase is not arrested by GroEL. Only a short lag phase at the beginning of reactivation and a slightly increased reactivation yield (64% to 86% for core-glycosylated and 62% to 76% for external invertase) indicate a weak interaction of the glycosylated forms with the chaperone.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | YEAST; OLIGOSACCHARIDES; RECONSTITUTION; GLYCOPROTEINS; CARBOXYLASE; AGGREGATION; MECHANISM; PROTEINS; INVITRO; ATP; CHAPERONE; GROE; FOLDING; AGGREGATION; GLYCOSYLATION; INVERTASE |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:44 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54465 |
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