Human fibrinogen and asialo-fibrinogen: a comparison of coagulation parameters. |
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Authors: | P A Gentry B Alexander |
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Institution: | Lindsley F. Kimball Research Institute, New York Blood Center, 310 East 67th Street, New York, New York 10021 U.S.A. |
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Abstract: | The effect of desialylation of fibrinogen on its conversion to fibrin has been investigated with particular reference to the kinetics of clot formation and structure. Also examined was the role of sialic acid in fibrinogen (factor I) poor in factor XIII (fibrinstabilizing factor) and factor I containing F XIII. The removal of more than 90% of the sialic acid of fibrinogen does not alter the thrombin clotting time, the clot solubility in monochloroacetic acid, the extent of cross-linking in the fibrin polymer, or the firmness and elasticity of the evolved clot. The data indicate that the sialic acid residues of fibrinogen do not contribute significantly to its conversion to fibrin by thrombin. |
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