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• W1529580689 startingPage "19040" @default.
• W1529580689 abstract "Platelets contain exceptionally high levels of pp60c-src and, thus, provide a convenient system for investigating the physiological function of this protein-tyrosine kinase. We have employed chemical cross-linking of myristylated amino-terminal peptides of pp60c-src to platelet membranes in order to identify platelet membrane components that interact with pp60c-src to regulate or mediate its activity. We detected specific binding of radioiodinated peptides to platelet membrane proteins of 32, 50, 92, and 105 kDa. The 32-kDa protein may be related to the putative src receptor component recently identified in fibroblast membranes. The most reactive platelet protein, however, is the 50-kDa protein, which is either absent or nonreactive in fibroblast membranes. Binding of src peptides to this protein was saturable, and we estimate the presence of approximately 1 x 10(6) of the 50-kDa binding sites per platelet. The specificity of the peptide binding to the 50- and 32-kDa platelet proteins was analyzed by competition with different peptides. The binding sites displayed an absolute requirement for an N-myristoyl moiety and a strong preference for pp60c-src amino-terminal sequences. The identification of these src-interacting proteins may help to decipher the biochemical pathways in which platelet pp60c-src is involved." @default.
• W1529580689 created "2016-06-24" @default.
• W1529580689 creator A5000844839 @default.
• W1529580689 creator A5089138950 @default.
• W1529580689 date "1991-10-01" @default.
• W1529580689 modified "2023-09-27" @default.
• W1529580689 title "Identification of platelet membrane proteins that interact with amino-terminal peptides of pp60c-src." @default.
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• W1529580689 doi "https://doi.org/10.1016/s0021-9258(18)55169-3" @default.
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