Effect of NaC1 on inactivation of bovine thrombin by antithrombin III in the presence of low affinity-heparin or dextran sulfate |
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| Authors: | G Oshima K Nagasawa |
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| Affiliation: | 1. College of Resources and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China;2. Hubei Key Laboratory for Efficient Utilization and Agglomeration of Metallurgic Mineral Resources, Wuhan University of Science and Technology, Wuhan, 430081, China;1. From the Department of Ophthalmology (H.S.), University of Minnesota, Minneapolis, Minnesota, USA;2. Department of Ophthalmology (A.V.Q.), Scripps Clinic, La Jolla, California, USA;3. Department of Ophthalmology/Bascom Palmer Eye Institute (E.A.V., R.K.P.II), University of Miami Miller School of Medicine, Miami, Florida, USA |
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| Abstract: | Heparin with low affinity (LA-heparin) to antithrombin III (AT III) enhanced the rate of inactivation of thrombin by AT III. The enhancement of the rate was saturable with AT III and was proportional to the LA-heparin concentration. Although the rate-enhancement in the presence of LA-heparin decreased with increase in NaC1 concentration, it was comparable with that in the presence of high affinity-heparin (HA-heparin) in the absence of NaC1. Inactivation of thrombin by AT III in the presence of dextran sulfate (DS) was also sensitive to NaC1 concentration. These findings indicate that free AT III is favorable for binding to the complexes of thrombin and highly sulfated polysaccharides having low affinities to AT III in the absence of NaC1. |
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