Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The non-ionic detergent Brij 58P is recommended as a stabilizing agent for protein storage; for example, the aggregation-prone chaperone DnaJ can be maintained in solution by low concentrations of Brij 58P. During protein folding studies with alpha-glucosidase, rhodanese and citrate synthase as model proteins, we discovered that the low concentrations of Brij 58P usually added with purified DnaJ to renaturation samples are sufficient to mimic chaperone effects with respect to prevention of protein aggregation. Furthermore, addition of Brij 58P to refolding alpha-glucosidase and citrate synthase enhanced the yield of refolded protein by a factor of two. Thus, Brij 58P can mimic chaperone effects and care should be taken when the substance is used to stabilize chaperone preparations.
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PMID:The non-ionic detergent Brij 58P mimics chaperone effects. 1245

The ubiquitous small heat shock proteins (sHsps) are efficient molecular chaperones that interact with nonnative proteins, prevent their aggregation, and support subsequent refolding. No obvious substrate specificity has been detected so far. A striking feature of sHsps is that they form large complexes with nonnative proteins. Here, we used several well established model chaperone substrates, including citrate synthase, alpha-glucosidase, rhodanese, and insulin, and analyzed their interaction with murine Hsp25 and yeast Hsp26 upon thermal unfolding. The two sHsps differ in their modes of activation. In contrast to Hsp25, Hsp26 undergoes a temperature-dependent dissociation that is required for efficient substrate binding. Our analysis shows that Hsp25 and Hsp26 reacted in a similar manner with the nonnative proteins. For all substrates investigated, complexes of defined size and shape were formed. Interestingly, several different nonnative proteins could be incorporated into defined sHsp-substrate complexes. The first substrate protein bound seems to determine the complex morphology. Thus, despite the differences in quaternary structure and mode of activation, the formation of large uniform sHsp-substrate complexes seems to be a general feature of sHsps, and this unique chaperone mechanism is conserved from yeast to mammals.
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PMID:Analysis of the interaction of small heat shock proteins with unfolding proteins. 1263 95