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Phosphorylation of glucokinase from rat liver in vitro by protein kinase A with a concomitant decrease of its activity

Ekman, Pia (author)
Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi,ek pia
Nilsson, Ewa (author)
Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi,ek pia
 (creator_code:org_t)
Elsevier BV, 1988
1988
English.
In: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861 .- 1096-0384. ; 261:2, s. 275-282
  • Journal article (peer-reviewed)
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  • 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

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Ekman, Pia
Nilsson, Ewa
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NATURAL SCIENCES
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Uppsala University

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