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Peptide fragments of myelin basic protein as substrates of protein kinase C.

Eller, Marika (author)
Uppsala universitet,Biokemi,Ulf Ragnarsson
Järv, Jaak (author)
Tartu universitet,Jaak Järv
Toomik, Reet (author)
Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,ek pia
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Ragnarsson, Ulf (author)
Uppsala universitet,Biokemi,Ragnarsson Ulf
Ekman, Pia (author)
Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,ek pia
Engström, Lorentz (author)
Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,engström lorentz
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 (creator_code:org_t)
1992
1992
English.
In: Biochemistry International. - 0158-5231. ; 27:4, s. 625-631
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

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

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