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• W2141330251 abstract "Human thrombomodulin (hTM) is a newly described endothelial cell associated protein that functions as a potent natural anticoagulant by converting thrombin from a procoagulant protease to an anticoagulant. The affinity constant of recombinant human soluble TM (rhs-TM) and a peptide containing active site of hTM fragment (f-hTM) with thrombin were determined using the surface plasmon resonance. The interaction of f-hTM with thrombin could be analyzed by a simple model, whereas the association and the dissociation steps of rhs-TM with thrombin consisted of at least two kinds of interaction phases. The dissociation constant for complex (KD) of f-hTM and thrombin was determined to be 205 nM, which was more than twice as high as that of rhs-TM (6.7 and 75 nM). The lower affinity of f-hTM was not due to the slow association rate but to the rapid dissociation rate. It comes clear that f-hTM interacts with thrombin rapidly. Am. J. Hematol. 63:136–140, 2000. © 2000 Wiley-Liss, Inc." @default.
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• W2141330251 date "2000-03-01" @default.
• W2141330251 modified "2023-10-18" @default.
• W2141330251 title "Study on complex formation between recombinant human thrombomodulin fragment and thrombin using surface plasmon resonance" @default.
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• W2141330251 doi "https://doi.org/10.1002/(sici)1096-8652(200003)63:3<136::aid-ajh5>3.0.co;2-i" @default.
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