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Tyrosine kinases in normal human blood cells
Author(s) -
Varshney Grish C.,
Kahn Axel,
Phan-Dinh-Tuy Françoise
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80873-0
Subject(s) - immunoprecipitation , tyrosine kinase , phosphorylation , proto oncogene tyrosine protein kinase src , monoclonal antibody , platelet , tyrosine , biochemistry , kinase , enzyme , microbiology and biotechnology , tyrosine phosphorylation , antibody , red blood cell , receptor tyrosine kinase , chemistry , biology , signal transduction , immunology , gene
The major tyrosine kinase from platelets was purified as a 51 kDa active enzyme which was shown to be a degradation product of the protooncogene product p60 c‐src . Immuno‐depletion experiments using a monoclonal antibody recognizing p60 c‐src failed to remove band 3 phosphorylating activity from red blood cell membranes. The erythrocyte tyrosine kinase was not at all immunoprecipitated by this antibody under conditions where the platelet enzyme was immunoprecipitated.