Characterization of monoclonal antibodies to human platelet myosin that recognize highly conserved epitopes within the 50 kDa fragment of myosin subfragment-1

Varda R. Deutsch*, Shakker Biadsi, Amiram Eldor, Andras Muhlrad, Itzhak Kahane

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Three monoclonal antibodies directed against human platelet myosin heavy chains (MCH) that recognize homologous sequences contained within the functionally active subfragment-1, in platelet and rabbit skeletal muscle myosin were studied. These antibodies are distinguished by their affinities to different myosins and their differential effect on various ATPase activities. Epitope mapping was accomplished by analyzing antibody binding to proteolytic peptides of myosin head subfragment-1 under various experimental conditions. The epitopes recognized by these anti-human platelet MHC monoclonal antibodies reside within a small region of the 50 kDa fragment, beginning 9 kDa from its C-terminus and extending a stretch of 6 kDa towards the N-terminus. These epitopes lie between residues 535-586, and are contained within a highly conserved area of myosin heavy chain.

Original languageEnglish
Pages (from-to)286-290
Number of pages5
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1038
Issue number3
DOIs
StatePublished - 8 May 1990

Keywords

  • Monoclonal antibody
  • Myosin
  • Myosin subfragment
  • Platelet

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