通过亲和色谱法分离人尿激肽释放酶。人尿激肽释放酶的测定，I。
Isolation of human urinary kallikrein by affinity chromatography. Determination of human urinary kallikrein, I.
作者信息
Geiger R, Mann K, Bettels T
出版信息
J Clin Chem Clin Biochem. 1977 Sep;15(9):479-83. doi: 10.1515/cclm.1977.15.1-12.479.
Human urinary kallikrein (EC 3.4.21.8) was purified to electrophoretically homogeneity by gel filtration on Sephadex G-100, followed by affinity chromatography on aprotinin-Sepharose. The molecular weight, estimated by gel filtration, is 64,000 Daltons, by dodecyl sulfate electrophoresis 45,000 Daltons and 29,000 Daltons, and it is microheterogeneous on electrofocusing, yielding isoelectric point values of 3.8, 3.9 and 4.05. The kinetic constants for hydrolysis of BZArgOEt, TosArgOMe, CbzTyrONp, and human HMW-kininogen were determined. Benzamidine and aprotinin are competitive inhibitors of human urinary kallikrein.
人尿激肽释放酶（EC 3.4.21.8）经葡聚糖凝胶G - 100凝胶过滤，随后在抑肽酶 - 琼脂糖上进行亲和层析，纯化至电泳纯。通过凝胶过滤估计分子量为64,000道尔顿，通过十二烷基硫酸盐电泳为45,000道尔顿和29,000道尔顿，并且在等电聚焦时具有微不均一性，等电点值为3.8、3.9和4.05。测定了对苄基精氨酸乙酯、甲苯磺酰精氨酸甲酯、苄氧羰基酪氨酸对硝基苯酯和人高分子量激肽原的水解动力学常数。苯甲脒和抑肽酶是人尿激肽释放酶的竞争性抑制剂。
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