Activation/dephosphorylation of muscle glycogen synthase phosphorylated by phosphorylase kinase

Ilona Parkas, P. Gergely

Research output: Contribution to journalArticle

Abstract

1. 1. Glycogen synthase from rabbit skeletal muscle was phosphorylated by phosphorylase kinase to yield synthase b2. 2. 2. Dephosphorylation and activation of synthase b2 by the catalytic subunits of protein phosphatase-1 (PP-lc) and protein phosphatase-2A (PP-2Ac) was studied. The apparent Km of PP-1c and PP-2Ac were 3. 3.3 μM and 6.2 μM, respectively. The apparent Vmax of PP-lc was about two times larger than that of PP-2Ac. 4. 4. Ligands with phosphate moiety (AMP, glucose-6-P at high concentration) caused an inhibition in dephosphorylation by both phosphatases. Spermine inhibited the dephosphorylation by PP-lc and stimulated the action of PP-2Ac. Therefore it can be employed to distinguish the phosphatases using synthase b2 as substrate.

Original languageEnglish
Pages (from-to)631-634
Number of pages4
JournalInternational Journal of Biochemistry
Volume21
Issue number6
DOIs
Publication statusPublished - 1989

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Phosphorylase Kinase
Glycogen Synthase
Phosphoric Monoester Hydrolases
Muscle
Chemical activation
Protein Phosphatase 1
Protein Phosphatase 2
Muscles
Spermine
Adenosine Monophosphate
Skeletal Muscle
Phosphates
Rabbits
Ligands
Glucose
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

Activation/dephosphorylation of muscle glycogen synthase phosphorylated by phosphorylase kinase. / Parkas, Ilona; Gergely, P.

In: International Journal of Biochemistry, Vol. 21, No. 6, 1989, p. 631-634.

Research output: Contribution to journalArticle

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