通过对α-胰蛋白酶抑制剂进行有限蛋白酶解衍生得到的Kunitz型蛋白酶抑制剂，II. 通过氨基酸序列测定对第二个抑制性失活结构域的表征。
Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, II. Characterization of a second inhibitory inactive domain by amino acid sequence determination.
作者信息
Wachter E, Hochstrasser K, Bretzel G, Heindl S
出版信息
Hoppe Seylers Z Physiol Chem. 1979 Sep;360(9):1297-303. doi: 10.1515/bchm2.1979.360.2.1297.
PMID:92448
Abstract
A short digestion with excess of trypsin releases an inhibitor with an apparent molecular weight of 14,000 from both the inter-alpha-trypsin inhibitor and the ITI-related acid-stable inhibitor. The amino acid sequence of this inhibitor was determined. The inhibitor is composed of two covalently linked homologous Kunitz-type domains. One domain has antitryptic activity, as reported. This paper characterizes the second, inactive domain as also of the Kunitz type.
摘要
用过量胰蛋白酶进行短时间消化，可从α-胰蛋白酶抑制剂和ITI相关酸稳定抑制剂中释放出一种表观分子量为14,000的抑制剂。测定了该抑制剂的氨基酸序列。该抑制剂由两个共价连接的同源Kunitz型结构域组成。如报道的那样，其中一个结构域具有抗胰蛋白酶活性。本文将第二个无活性结构域也鉴定为Kunitz型。
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