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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1992 Apr 1;89(7):2888–2892. doi: 10.1073/pnas.89.7.2888

Photoaffinity labeling of the primary fibrin polymerization site: isolation and characterization of a labeled cyanogen bromide fragment corresponding to gamma-chain residues 337-379.

A Shimizu 1, G M Nagel 1, R F Doolittle 1
PMCID: PMC48768  PMID: 1557395

Abstract

Human fibrinogen and the plasmin-generated fibrinogen fragment D were photoaffinity labeled specifically with the peptide [14C]Gly-Pro-Arg-N(4-azido-2-nitrophenyl)Lys amide. In the case of fibrinogen, greater than 85% of the incorporated radioactivity was found in the gamma chain. Similarly, when fragment D (Mr, 90,000) was labeled with the same derivatized peptide, virtually all the radioactivity was found in the gamma-chain portion. The labeled fragment D was treated with CNBr and an initial purification was achieved by two gel-filtration steps. The labeled material was purified further by HPLC and was also compared with CNBr digests of unlabeled material. Amino acid analysis and gas-phase sequencing showed the labeled fragment to be gamma-chain residues 337-379.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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