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- W1964643048 abstract "Rapid and efficient purification methods that include hydrophobic chromatography on Phenyl Sepharose CL-4B have been developed for the peptides that span residues 241-476 (CNBr VIII), and 518-584 (CNBr X) in the A alpha chain of human fibrinogen. Amino acid analysis, NH2-terminal sequence determination, and SDS-PAGE indicated that greater than 95% purity of each peptide was achieved. Sensitive and specific radioimmunoassays capable was achieved. Sensitive and specific radioimmunoassays capable of detecting antigen in the range of 0.1-10.0 pmol/ml have also been developed for CNBr VIII and CNBr X. These assays have been characterized and successfully applied in studies designed to localize the two COOH-terminal A alpha chain regions in column effluents of CNBr-digested fibrinogen and crosslinked fibrin. When these immunoassays were used to study purified preparations of a high molecular weight, crosslink-containing CNBr derivative of a alpha polymer, the data provided immunologic confirmation for the involvement of CNBr VIII and CNBr X in alpha chain crosslinking." @default.
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- W1964643048 date "1982-06-01" @default.
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- W1964643048 title "Alpha chain crosslinking of human fibrin: Purification and radioimmunoassay development for two Aα chain regions involved in crosslinking" @default.
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- W1964643048 doi "https://doi.org/10.1016/0049-3848(82)90313-9" @default.
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