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Peptide fragments of myelin basic protein as substrates of protein kinase C.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Ulf Ragnarsson)
Tartu universitet. (Jaak Järv)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. (ek pia)
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Ragnarsson Ulf)
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1992 (English)In: Biochemistry International, ISSN 0158-5231, Vol. 27, no 4, 625-631 p.Article in journal (Refereed) Published
Abstract [en]

A set of peptides derived from myelin basic protein was synthesized and the kinetics of their phosphorylation by protein kinase C was studied. The replacement or the removal of the N-terminal Gln had no effect on the activity of the parent peptide. The removal of the following Lys or Arg led to a systematic decrease in substrate activity. The modifications in the C-terminal part of the peptide had a weaker influence on the parameters Vmax and KM than those in the N-terminal. The rather regular dependence of the activity of substrates upon their structure does not allow the strict definition of a minimum substrate for protein kinase C.

Place, publisher, year, edition, pages
1992. Vol. 27, no 4, 625-631 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-173138PubMedID: 1384495OAI: oai:DiVA.org:uu-173138DiVA: diva2:516713
Available from: 2012-04-19 Created: 2012-04-19 Last updated: 2012-04-19Bibliographically approved

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