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. 1969 Aug;63(4):1247–1252. doi: 10.1073/pnas.63.4.1247

INTRAMOLECULAR LOCALIZATION OF THE ACCEPTOR CROSS-LINKING SITES IN FIBRIN*

L Lorand 1, D Chenoweth 1
PMCID: PMC223457  PMID: 5260927

Abstract

Using 1-14C-glycine ethyl ester to titrate and label the acceptor cross-linking sites in fibrin, it was possible to localize and characterize the reactivity of these sites. In terms of sulfitolyzed chain fragments, both α and γ chains were shown to act as amine-acceptors, the site in γ being more reactive. Identification and isolation of the acceptor loci were also achieved after cyanogen bromide fragmentation. It is interesting that the “N-terminal disulfide knot” portion of fibrin does not seem to contain acceptor functions.

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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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