牛垂体中主要阳离子激肽释放酶抑制剂的纯化与特性分析
Purification and characterization of the major cationic kallikrein inhibitor in bovine pituitary gland.
作者信息
Ikekita M, Jone C S, Kamo M, Tsugita A, Kizuki K, Moriya H
机构信息
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo, Japan.
出版信息
Protein Seq Data Anal. 1992;5(1):7-11.
The presence of two types of kallikrein inhibitor (cationic and anionic inhibitors) was demonstrated in bovine pituitary gland. These kallikrein inhibitors were separated from the homogenate of bovine posterior pituitary by successive CM-Sephadex chromatography. The major cationic inhibitor was further purified to homogeneity by affinity chromatography using porcine pancreatic beta-kallikrein immobilized on Sepharose 4B and gel filtration. The complete amino acid sequence of this inhibitor was first determined, and it was shown to be a peptide of 58 residues with a calculated molecular weight of 6,511. The Ki value against bovine pituitary kallikrein was 6 x 10(-9) M. The cationic inhibitor was found to be identical with basic pancreatic trypsin inhibitor.
在牛垂体中证实存在两种激肽释放酶抑制剂（阳离子抑制剂和阴离子抑制剂）。通过连续的CM - 葡聚糖凝胶柱色谱法从牛垂体后叶匀浆中分离出这些激肽释放酶抑制剂。使用固定在琼脂糖4B上的猪胰β - 激肽释放酶通过亲和色谱法和凝胶过滤将主要的阳离子抑制剂进一步纯化至同质。首先确定了该抑制剂的完整氨基酸序列，结果表明它是一个由58个残基组成的肽，计算分子量为6511。其对牛垂体激肽释放酶的Ki值为6×10⁻⁹ M。发现该阳离子抑制剂与碱性胰蛋白酶抑制剂相同。
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