Influence of osmolytes on inactivation and aggregation of muscle glycogen phosphorylase b by guanidine hydrochloride. Stimulation of protein aggregation under crowding conditions

Biochemistry (Mosc). 2005 Sep;70(9):1020-6. doi: 10.1007/s10541-005-0219-8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Betaine / metabolism
  • Betaine / pharmacology
  • Dose-Response Relationship, Drug
  • Glycine / metabolism
  • Glycine / pharmacology
  • Glycogen Phosphorylase, Muscle Form / metabolism*
  • Guanidine / pharmacology*
  • Kinetics
  • Methylamines / metabolism
  • Methylamines / pharmacology
  • Muscle, Skeletal / drug effects
  • Muscle, Skeletal / enzymology
  • Proline / metabolism
  • Proline / pharmacology
  • Rabbits

Substances

  • Methylamines
  • Betaine
  • Proline
  • Glycogen Phosphorylase, Muscle Form
  • trimethyloxamine
  • Guanidine
  • Glycine