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Chemical modification of 6 lysyl residues within the B-chain of alpha-thrombin was decreased on binding of equal molar hirudin, a thrombin-specific inhibitor. They are Lys-B21 (87% protected), Lys-B52 (80%), Lys-B65 (greater than 95%), Lys-B106 (71%), Lys-B107 (71%), and Lys-B154 (80%). The data suggest that these lysyl residues are situated within or in close proximity to the hirudin-binding site of human alpha-thrombin.
Jia‐Yaw Chang (1989) studied this question.