不正常的凝血酶的凝血酶原德岛:描述来自人类凝血酶原的一个变种。
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川内Inomoto T, Shirakami,年代,Shigekiyo T,齐藤年代,三好K,盛田昭夫T, Iwanaga年代
不正常的凝血酶的凝血酶原德岛:描述来自人类凝血酶原的一个变种。
血。1987年2月,69 (2):565 - 9。
- PubMed ID
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3801671 (在PubMed]
- 文摘
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凝血酶原基因突变,指定的凝血酶原德岛,从等离子体净化的渊源者正常血浆凝血活动的12%和42%的正常的凝血酶原抗原。纯化制备了一个乐队的流动一样,“凝血酶原”,十二烷基硫酸钠聚丙烯酰胺凝胶电泳(sds - page)。因子Xa-catalyzed蛋白质水解的凝血酶原德岛发现了sds - page是相同的,“凝血酶原。”Subsequently thrombin Tokushima was prepared by CM-Sepharose CL-6B column chromatography after prothrombin activation by factor Xa. The molecular weight of thrombin Tokushima estimated by SDS-PAGE was identical to that of "thrombin." Thrombin Tokushima exhibited less than 22% of normal clotting activity, and the value of kcat/Km (mumol/L-1 second-1) was less than one tenth of that of "thrombin" when Boc-Val-Pro-Arg-4-methylcoumaryl-7-amide was used as a substrate. However, active site titration using p-nitrophenyl-p'-guanidinobenzoate failed to detect any difference between the two. Thrombin Tokushima was 2.5% as effective as "thrombin" in inducing platelet aggregation. Interaction of thrombin Tokushima with antithrombin III was much slower than "thrombin" when followed by SDS-PAGE. Based on the residual thrombin activity, it was 33% as effective as "thrombin" in forming a complex with antithrombin III. These results indicate that the molecular defect resides in the thrombin portion of prothrombin Tokushima and that the binding sites for various substrates appear to be greatly impaired.