Kunitz-type protease inhibitor found in rat mast cells. Purification, properties, and amino acid sequence.
Kunitz-type protease inhibitor found in rat mast cells. Purification, properties, and amino acid sequence.
复制标题
在大鼠肥大细胞中发现的库尼茨型蛋白酶抑制剂。
DOI：
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发表时间：
1988
影响因子：
4.8
通讯作者：
N. Katunuma
中科院分区：
文献类型：
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作者：
H. Kido;Y. Yokogoshi;N. Katunuma
A low molecular weight serine protease inhibitor, named trypstatin, was purified from rat peritoneal mast cells. It is a single polypeptide with 61 amino acid residues and an Mr of 6610. Trypstatin markedly inhibits blood coagulation factor Xa (Ki = 1.2 x 10(-10) M) and tryptase (Ki = 3.6 x 10(-10) M) from rat mast cells, which have activities that convert prothrombin to thrombin. It also inhibits porcine pancreatic trypsin (Ki = 1.4 x 10(-8) M) and chymase (Ki = 2.4 x 10(-8) M) from rat mast cells, but not papain, alpha-thrombin, or porcine pancreatic elastase. Trypstatin forms a complex in a molar ratio of 1:1 with trypsin and one subunit of tryptase. The complete amino acid sequence of this inhibitor was determined and compared with those of Kunitz-type inhibitors. Trypstatin has a high degree of sequence homology with human and bovine inter-alpha-trypsin inhibitors, A4(751) Alzheimer's disease amyloid protein precursor, and basic pancreatic trypsin inhibitor. However, unlike other known Kunitz-type protease inhibitors, it inhibits factor Xa most strongly.
