The polymerization of proteins: the action of thrombin on fibrinogen

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Abstract

Viscosity measurements and ultracentrifugal experiments show no difference between fibrinogen and fibrinogen incubated with thrombin, both kept at pH 4.85, although the progressing action of thrombin can be demonstrated.

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    First, Elemer Mihalyi performed elegant analytical studies that showed that the electrophoretic mobilities of fibrinogen and fibrin dispersed in urea were different, the former being more negatively charged [2]. Shortly thereafter, Koloman Laki found that when fibrinogen was treated with thrombin at low pH, no gel formed [3]. Finally, in a joint publication, the laboratories of Kenneth Bailey and Lazlo Lorand reported that the amino-terminals of fibrinogen and fibrin were different [4], in particular new glycine endgroups appearing presumably as the result of peptide material being released from fibrinogen by the action of thrombin.

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    We precipitated fibrinogen with ammonium sulfate (30% sat), dissolved it in phosphate-buffered saline (PBS) (1/5 original volume), and re-precipitated twice with 2.1 m glycine. We dissolved the precipitate in 0.1 m Na phosphate buffer, pH 6.4 (1/10 original volume), added an equal volume of water, and incubated the solution overnight at 4 °C to remove cold-insoluble material [33], then added ε-aminocaproic acid (0.1 m) to the supernate, precipitated FXIII-rich plasminogen-free fraction I-2 fibrinogen at 30% saturated ammonium sulfate, then re-dissolved in Tris-buffered saline (TBS), pH 7.0 buffer containing Trasylol, 10 μ mL−1 (coagulability >96%). Human fibrinogen I-2 was prepared as described [34].

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    Although Hammarsten first purified fibrinogen from horse plasma in 1876 (Blombäck, 2001), human fibrinogen was isolated in large quantities only fifty years ago (Cohn et al., 1946) and has been extensively studied since then. Fibrinogen and the other components of the clotting system are commonly isolated from human blood plasma, using purification methods based on fibrinogen's low solubility in various solvents or its isoelectric point (Blombäck and Blombäck, 1956; Cohn et al., 1946; Laki, 1951). Fibrinogen was last reviewed in this series in 1973 (Doolittle, 1973).

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1

Public Health Service Visiting Scientist of the Experimental Biology and Medicine Institute.

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