水解肽激素缓激肽的兔组织肽酶。兔组织中酶特性和浓度的差异。
Rabbit tissue peptidases that hydrolyse the peptide hormone bradykinin. Differences in enzymic properties and concentration in rabbit tissues.
作者信息
Cicilini M A, Caldo H, Berti J D, Camargo A C
出版信息
Biochem J. 1977 Jun 1;163(3):433-9. doi: 10.1042/bj1630433.
The distribution and properties of neutral peptidases acting on the peptide hormone bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) were determined in several rabbit tissues. The supernatant and particulate fractions prepared from tissue homogenates (25000g for 60min) were studied. Bradykinin inactivation (kininase activity) was measured by bioassay with the isolated guinea-pig ileum. The sites of peptide-bond cleavage were determined in the amino acid analyser, which permits detection and measurement of amino acids and peptides derived from bradykinin. The results indicate that kininases are present in a wide range of concentrations in different tissues, kidney and lung having the most activity. Kininases present in different tissues were distinguished on the basis of sensitivity to the effects of EDTA, dithiothreitol and ZnCl2 and by the site of peptide-bond hydrolysis in bradykinin.
在几种兔组织中测定了作用于肽激素缓激肽（精氨酸-脯氨酸-脯氨酸-甘氨酸-苯丙氨酸-丝氨酸-脯氨酸-苯丙氨酸-精氨酸）的中性肽酶的分布和特性。研究了从组织匀浆（25000g离心60分钟）制备的上清液和颗粒部分。通过对分离的豚鼠回肠进行生物测定来测量缓激肽失活（激肽酶活性）。在氨基酸分析仪中确定肽键裂解位点，该分析仪可检测和测量源自缓激肽的氨基酸和肽。结果表明，激肽酶在不同组织中的浓度范围很广，肾脏和肺的活性最高。根据对EDTA、二硫苏糖醇和ZnCl2作用的敏感性以及缓激肽中肽键水解的位点，区分了不同组织中存在的激肽酶。
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