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

Renné Chen | Zendy; Russell F. Doolittle | Zendy

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

Author(s) -

Renné Chen,

Russell F. Doolittle

Publication year - 1970

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.66.2.472

Subject(s) - fibrin , chemistry , biochemistry , acceptor , cleavage (geology) , amino acid residue , peptide sequence , amino acid , biology , immunology , gene , paleontology , physics , fracture (geology) , condensed matter physics

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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