Multiple active forms of thrombin. I. Partial resolution, differential activities, and sequential formation.
Multiple active forms of thrombin. I. Partial resolution, differential activities, and sequential formation.
复制标题
凝血酶的多种活性形式。
DOI：
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发表时间：
1971
影响因子：
4.8
通讯作者：
D. Fass
中科院分区：
文献类型：
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作者：
K. Mann;C. Heldebrant;D. Fass
摘要：用硫乙基Sephadex对凝血酶的两大分子量进行了色谱分离。较大的凝血酶是一个39000道尔顿的分子，由33000道尔顿和6000道尔顿的两条二硫链组成。较小的凝血酶的完整分子量为28000。至少有两种分子种类包含在这一类中，它们具有(a) 18,000和10,000道尔顿以及(b) 14,000, 4,000和10,000道尔顿。所有分离的凝血酶对甲酰基精氨酸甲酯具有相同的特异性活性。较大的凝血酶的凝血比活性为每毫克2700 NIH单位，而两种较小的凝血酶的凝血比活性似乎分别为该值的0.50和0.25。用Parke-Davis局部凝血酶和部分纯化的凝血酶原进行的研究表明，较小的凝血酶是由较大的凝血酶依次产生的。
Abstract The two major molecular weight classes of thrombin have been resolved chromatographically on sulfoethyl Sephadex. The larger thrombin is a molecule of 39,000 daltons, composed of two disulfide-linked chains of 33,000 and 6,000 daltons. The smaller thrombins have an intact molecular weight of 28,000. At least two molecular species are contained in this class with the proposed disulfide-linked chain structure (a) 18,000 and 10,000 daltons and (b) 14,000, 4,000, and 10,000 daltons. All the thrombins isolated have identical specific activities toward tosyl-l-arginine methyl ester. The clotting specific activity of the larger thrombin is 2,700 NIH units per mg while those of the two smaller thrombins appear to be about 0.50 and 0.25 of this value, respectively. Studies conducted with Parke-Davis topical thrombin and partially purified prothrombin indicate that the smaller thrombins are sequentially produced from the larger thrombin.