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Literature summary extracted from

  • Eronina, T.B.; Chebotareva, N.A.; Kurganov, B.I.
    Influence of osmolytes on inactivation and aggregation of muscle glycogen phosphorylase b by guanidine hydrochloride. Stimulation of protein aggregation under crowding conditions (2005), Biochemistry (Moscow), 70, 1020-1026.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.4.1.1 biotechnology study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation. Test system for the study of the effects of macromolecular crowding induced by osmolytes on aggregation of proteins Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.1 guanidine hydrochloride study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Oryctolagus cuniculus
-
 isoform phosphorylase b
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.4.1.1 study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation. Test system for the study of the effects of macromolecular crowding induced by osmolytes on aggregation of proteins Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.1 muscle skeletal muscle Oryctolagus cuniculus
-