Recognition site for the platelet receptor is present on the 15-residue carboxy-terminal fragment of the gamma chain of human fibrinogen and is not involved in the fibrin polymerization reaction.

@article{Kloczewiak1983RecognitionSF,
  title={Recognition site for the platelet receptor is present on the 15-residue carboxy-terminal fragment of the gamma chain of human fibrinogen and is not involved in the fibrin polymerization reaction.},
  author={M Kloczewiak and Sheila Timmons and Jack Hawiger},
  journal={Thrombosis research},
  year={1983},
  volume={29 2},
  pages={249-55}
}
A pentadecapeptide, derived from a staphylococcal protease digest of the 27-residue carboxy-terminal cyanogen bromide fragment of human fibrinogen gamma chain, inhibits binding of 125I-fibrinogen to human platelet receptors and aggregation of platelets induced by ADP and fibrinogen. Amino acid composition and NH2 terminal analysis indicate that the isolated pentadecapeptide corresponds to residues 397 to 411 of the gamma chain. A synthetic peptide also inhibited binding of 125I-fibrinogen and… CONTINUE READING

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