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Phosphorylation of glucokinase from rat liver in vitro by protein kinase A with a concomitant decrease of its activity
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
1988 (English)In: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 261, no 2, 275-282 p.Article in journal (Refereed) Published
Abstract [en]

Glucokinase, purified from rat liver, was phosphorylated to an extent of 1 mol [32P]-phosphate/mol of enzyme when incubated with [32P]ATP and protein kinase A from pig or rabbit muscle. The phosphate was bound to serine residues. K0.5 increased and Vmax decreased upon phosphorylation. The phosphate group was removed during incubation of the phosphorylated glucokinase with alkaline phosphatase. Enzymatically inactive glucokinase was not phosphorylated by the protein kinase.

Place, publisher, year, edition, pages
1988. Vol. 261, no 2, 275-282 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-172751DOI: 10.1016/0003-9861(88)90342-6OAI: oai:DiVA.org:uu-172751DiVA: diva2:515543
Available from: 2012-04-13 Created: 2012-04-13 Last updated: 2017-12-07Bibliographically approved

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