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Phosphorylation of ...
Phosphorylation of glucokinase from rat liver in vitro by protein kinase A with a concomitant decrease of its activity
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- Ekman, Pia (author)
- Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi,ek pia
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- Nilsson, Ewa (author)
- Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi,ek pia
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(creator_code:org_t)
- Elsevier BV, 1988
- 1988
- English.
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In: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861 .- 1096-0384. ; 261:2, s. 275-282
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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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)
Publication and Content Type
- ref (subject category)
- art (subject category)
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