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The Identification of Fibrinopeptide B as a Chemotactic Agent Derived from Human Fibrinogen
Author(s) -
Kay A. B.,
Pepper D. S.,
McKenzie Robin
Publication year - 1974
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1974.tb06633.x
Subject(s) - chemotaxis , fibrinogen , thrombin , chemistry , peptide , biochemistry , venom , snake venom , microbiology and biotechnology , platelet , immunology , biology , receptor
Chemotactic activity for human peripheral blood leucocytes was generated by the action of thrombin on human fibrinogen, a reaction known to release low molecular weight fibrinopeptides. Following gel filtration of the clot supernatant most of the activity eluted at the same K d as synthetic fibrinopeptides. Fibrinopeptides present in the clot supernatant were then identified and separated by high voltage electrophorcsis in two dimensions. Chemotactic activity was a property of fibrinopeptide B and not of fibrinopeptides A, AP or AY. Supernatants prepared with contortrix venom, which cleaves the B peptide, were also chemotactic whereas no activity was present in supernatants prepared from Arvin venom which cleaves peptides A, AP and AY. Synthetic fibrinopeptide B and a B analogue, 1‐glutamic acid, were found to be chemotactic but not synthetic fibrinopeptide A. Thus chemotaxis of human leucocytes represents a further biological activity of fibrinopeptide B.