Immunochemical Studies of Aα Chain Crosslinking
Nearly two decades ago our colleague, the late Dr. Hymie Nossel, considered the possibility that radioimmunoassays might have as much application in the field of coagulation as they had been shown to have in the field of endocrinology. He selected fibrinopeptide A as a likely candidate for measurement (1) and initiated a new era in the quantitation of peptides or proteins that are biochemical markers for various aspects of the coagulation process.
KeywordsCyanogen Bromide High Molecular Weight Polymer Human Fibrinogen Fibrin Monomer Immunochemical Study
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- 5.R. F. Doolittle, K. G. Cassman, B. A. Cottrell, and S. J. Friezner, Amino acid sequence studies on the α chain of human fibrinogen: Isolation and characterization of two linked α-chain cyanogen bromide fragments from fully crosslinked fibrin. Biochemistry, 16:1715–1719 (1977b).CrossRefGoogle Scholar
- 11.C. W. Francis, V. J. Marder, and S. E. Martin, Plasmic degradation of crosslinked fibrin I. Structural analysis of the particulate clot and identification of new macro-molecular soluble complexes. Blood, 56:456–464 (1980a).Google Scholar
- 13.J. H. Sobel, C. A. Thibodeau, and R. E. Canfield, Early alpha chain crosslinking in human fibrin preparations. Thromb. Haemostasis, 60:153–159 (1988).Google Scholar
- 14.J. H. Sobel, C. A. Thibodeau, M. A. Gawinowicz Kolks, and R. E. Canfield, Immunochemical characterization of crosslinked derivatives isolated from alpha chain oligomers formed during early stages of fibrin crosslinking. Thromb. Haemostasis, 60:160–169 (1988).Google Scholar
- 15.J. H. Sobel, H. Backus, and R. E. Canfield, Immunodetection of rt-PA-mediated fibrino(geno)lysis using monoclonal antibodies that recognize (A)α chain crosslinking regions. Thromb. Haemostasis, 62:73 (abst.) (1989).Google Scholar
- 17.J. H. Sobel, C. A. Thibodeau, M. A. Gawinowicz Kolks, and R. E. Canfield, The equine fibrinogen Aα chain: Partial structural comparison with human Aα chain crosslinking regions. in Fibrinogen 3. Biochemistry, biologic functions, gene regulation and expression. M. W. Mosesson, et al. eds. Elsevier Science Publishers, B. V. (1988).Google Scholar