Regulation of the dephosphorylation of phosphorylase A by glucose, AMP and polyamines

Ilona Farkas, Béla Tóth, P. Gergely

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

1. 1. The effect of glucose, caffeine, AMP and polyamines was investigated on the dephosphorylation of phosphorylase a by the catalytic subunits of protein phosphatase-1 and -2A. 2. 2. Caffeine at 1-20 μM inhibited the dephosphorylation of the dimeric phosphorylase a at 37°C using skeletal muscle enzymes; 0.1-10 mM of caffeine enhanced the rate of dephosphorylation greatly at 13°C and slightly at 37°C. 3. 3. α-d-Glucose was more effective in accelerating both the dephosphorylation and the tryptic digestion of phosphorylase a than the β-anomer. 4. 4. Polyamines were found to moderate the inhibitory effect of AMP at concentrations which may occur in the tissues. In the presence of 5 mM glucose polyamines could cancel the AMP inhibition of the dephosphorylation of liver phosphorylase a by hepatic protein phosphatase-1 and -2A.

Original languageEnglish
Pages (from-to)197-201
Number of pages5
JournalInternational Journal of Biochemistry
Volume20
Issue number2
DOIs
Publication statusPublished - 1988

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Phosphorylase a
Phosphorylases
Polyamines
Adenosine Monophosphate
Caffeine
Protein Phosphatase 1
Glucose
Protein Phosphatase 2
Liver
Muscle
Digestion
Skeletal Muscle
Tissue
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

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Regulation of the dephosphorylation of phosphorylase A by glucose, AMP and polyamines. / Farkas, Ilona; Tóth, Béla; Gergely, P.

In: International Journal of Biochemistry, Vol. 20, No. 2, 1988, p. 197-201.

Research output: Contribution to journalArticle

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