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Influence of Osmolytes on Inactivation and Aggregation of Muscle Glycogen Phosphorylase b by Guanidine Hydrochloride. Stimulation of Protein Aggregation under Crowding Conditions
Authors:T.?B.?Eronina  author-information"  >  author-information__contact u-icon-before"  >  mailto:eronina@inbi.ras.ru"   title="  eronina@inbi.ras.ru"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author,N.?A.?Chebotareva,B.?I.?Kurganov
Affiliation:(1) Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia
Abstract:The effects of the osmolytes trimethylamine-N-oxide (TMAO), betaine, proline, and glycine on the kinetics of inactivation and aggregation of rabbit skeletal muscle glycogen phosphorylase b by guanidine hydrochloride (GuHCl) have been studied. It is shown that the osmolytes TMAO and betaine exhibit the highest protective efficacy against phosphorylase b inactivation. A test system for studying the effects of macromolecular crowding induced by osmolytes on aggregation of proteins is proposed. TMAO and glycine increase the rate of phosphorylase b aggregation induced by GuHCl.
Keywords:muscle glycogen phosphorylase b   guanidine hydrochloride  inactivation  aggregation  osmolyte
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