探究水蛭素两个结合位点之间的距离，以了解其与α-凝血酶活性位点及纤维蛋白（原）结合位点的相互作用。
Probing the distance between the two binding sites of hirudin for its interaction with the active site and the fibrin(ogen)-binding site of alpha-thrombin.
作者信息
Wagner U, Schmitz T, Otte M, Dodt J
机构信息
Institut für Biochemie, Technische Hochschule Darmstadt.
出版信息
Biomed Biochim Acta. 1991;50(4-6):707-10.
PMID:1801747
Abstract
The interaction of delta (Ser50)-hirudin with alpha-thrombin has been investigated. Deletion of Ser50 of r-hirudin caused a 2.7 fold increase of the Ki for its complex with alpha-thrombin. Determination of the rate constants kon and koff for complex formation showed that this effect was mainly due to a change in koff.
摘要
已对δ（Ser50）-水蛭素与α-凝血酶的相互作用进行了研究。r-水蛭素Ser50的缺失导致其与α-凝血酶形成复合物的Ki增加了2.7倍。复合物形成的速率常数kon和koff的测定表明，这种效应主要是由于koff的变化。
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