The hirudin-binding site of human alpha-thrombin. Identification of lysyl residues which participate in the combining site of hirudin-thrombin complex.
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.
Chang
J Y
JY
Pharmaceuticals Research Laboratories, CIBA-GEIGY Ltd., Basel, Switzerland.
D000595:Amino Acid Sequence; D001557:Benzenesulfonates; D001665:Binding Sites; D002850:Chromatography, Gel; D004396:Coloring Agents; D006629:Hirudins / Q000378:metabolism*; D006801:Humans; D008239:Lysine; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D011994:Recombinant Proteins; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000037:antagonists & inhibitors / Q000378:metabolism*
D001557:Benzenesulfonates; D004396:Coloring Agents; D006629:Hirudins; D011994:Recombinant Proteins; D013917:Thrombin; D008239:Lysine