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PNAS | June 15, 1970 | vol. 66 | no. 2 | 472-479
Copyright © 1970 by the National Academy of Sciences

Isolation, Characterization, and Location of a Donor-Acceptor Unit from Cross-Linked Fibrin

Renne Chen and Russell F. Doolittle

The cross-linking systems of bovine and human fibrins were studied by the introduction of a radioactive substitute donor as an inhibitor of fibrin cross-linking, separation of the constituent polypeptide chains after sulfitolysis, and tryptic digestion of the labeled gamma -chains. The information gathered from this approach enabled us to isolate and characterize the complete donor-acceptor unit in tryptic digests of fibrin gamma -gamma cross-linked systems. In both bovine and human fibrin, this kind of cross-linking is accomplished by reciprocal bridging between overlapping carboxy-terminal segments of neighboring gamma -chains. The amino acid sequence of the carboxy-terminal heptadecapeptide of the bovine gamma -chain was determined and an alignment of the corresponding region of the human gamma -chain established.
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