Influence of osmolytes on inactivation and aggregation of muscle glycogen phosphorylase b by guanidine hydrochloride. Stimulation of protein aggregation under crowding conditions.
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.
Eronina
T B
TB
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia. eronina@inbi.ras.ru
Chebotareva
N A
NA
Kurganov
B I
BI
D000818:Animals; D001622:Betaine / Q000378:metabolism / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D005998:Glycine / Q000378:metabolism / Q000494:pharmacology; D024982:Glycogen Phosphorylase, Muscle Form / Q000378:metabolism*; D019791:Guanidine / Q000494:pharmacology*; D007700:Kinetics; D008744:Methylamines / Q000378:metabolism / Q000494:pharmacology; D018482:Muscle, Skeletal / Q000187:drug effects / Q000201:enzymology; D011392:Proline / Q000378:metabolism / Q000494:pharmacology; D011817:Rabbits
D008744:Methylamines; D001622:Betaine; D011392:Proline; D024982:Glycogen Phosphorylase, Muscle Form; C005855:trimethyloxamine; D019791:Guanidine; D005998:Glycine