将马血清中的第二种α-2-抗蛋白酶鉴定为抗凝血酶III。

Identification of the second alpha-2-antiprotease of equine serum as antithrombin III.

作者信息

Pellegrini A, Zweifel H R, von Fellenberg R

出版信息

Int J Biochem. 1983;15(7):917-22. doi: 10.1016/0020-711x(83)90167-2.

Abstract

The alpha-2-protease inhibitor, of 65,000 daltons molecular weight, described by several authors in horse plasma and also present as a contaminant in alpha-1-isoinhibitor isolates previously described by us (Pellegrini & von Fellenberg (1980) Biochim. biophys. Acta 616, 351-361) has now been isolated to purity and identified as antithrombin III. The inhibitor is composed of a single polypeptide chain as judged by SDS polyacrylamide gel electrophoresis. The inhibitor was effective only against trypsin and thrombin. Serological cross-reaction existed between the inhibitor and the antiserum to human antithrombin III. An antiserum to our isolate, however, did not react with human antithrombin III. This confirms the results reported by Kurachi et al. (1976, Biochemistry 15, 368-372).

摘要

几位作者在马血浆中描述的分子量为65,000道尔顿的α-2-蛋白酶抑制剂，也是我们之前描述的α-1-异抑制剂分离物中的污染物（佩莱格里尼和冯·费伦贝格（1980年）《生物化学与生物物理学报》616卷，351 - 361页），现已被分离至纯品，并鉴定为抗凝血酶III。通过SDS聚丙烯酰胺凝胶电泳判断，该抑制剂由一条单一多肽链组成。该抑制剂仅对胰蛋白酶和凝血酶有效。该抑制剂与抗人抗凝血酶III血清之间存在血清学交叉反应。然而，针对我们分离物的抗血清与人类抗凝血酶III不发生反应。这证实了仓知等人（1976年，《生物化学》15卷，368 - 372页）报道的结果。