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Monoclonal-antibodies to protein kinase-c-gamma - functional-relationship between epitopes and cofactor binding-sites

Academic Article
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Overview

authors

  • Cazaubon, S.
  • Marais, R.
  • Parker, P.
  • Strosberg, Donny

publication date

  • June 1989

journal

  • European Journal of Biochemistry  Journal

abstract

  • Four monoclonal antibodies (mAbs), derived from high-responder Biozzi mice immunized with purified protein kinase C, were selected by ELISA and further characterized by immunoblot: 3G12, 5A2, 36G9 are of isotype gamma 1, kappa and 15G4 is of isotype gamma 2b, kappa. Competition analysis between 15G4 and the three other mAbs showed that 15G4 and 3G12 are directed against either the same or overlapping epitope(s). All four mAbs are specific for the bovine gamma isoform of protein kinase C and cross-react with protein kinase C gamma from a variety of animal species. Immunoblot analysis of protein kinase C tryptic fragments revealed that the mAbs recognize the regulatory domain and not the catalytic domain. Two of the mAbs, 36G9 and 5A2, inhibit protein kinase C gamma cofactor-dependent activity (80% and 50% respectively). Consistent with the epitope mapping, none of mAbs inhibit the cofactor-independent catalytic activity of protein kinase C gamma. Competition analysis between these mAbs and phosphatidylserine, 12-O-tetradecanoylphorbol 13-acetate and Ca2+ showed that 36G9 and 5A2 block cofactor binding to protein kinase C gamma. These four mAbs thus interact with at least three distinct epitopes in the regulatory domain of protein kinase C gamma.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Antibody Formation
  • Binding Sites, Antibody
  • Binding, Competitive
  • Blotting, Western
  • Cattle
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes
  • Peptide Fragments
  • Precipitin Tests
  • Protein Kinase C
  • Species Specificity
  • Structure-Activity Relationship
  • Trypsin
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Identity

International Standard Serial Number (ISSN)

  • 0014-2956

Digital Object Identifier (DOI)

  • 10.1111/j.1432-1033.1989.tb14845.x

PubMed ID

  • 2472272
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Additional Document Info

start page

  • 401

end page

  • 406

volume

  • 182

issue

  • 2

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