RENAL ENZYMES THAT REGULATE BLOOD PRESSURE

肾酶及其激活剂的研究将是 继续强调组织激肽释放酶和肾素。虽然 这些酶集中在肾脏，它们存在于 其他器官也是如此。破译的最新进展 肾素原和激肽释放酶原的结构使其有可能 确立激活模式，识别内生激活 失活的酶原酶。这两者都被激活了 均一原激肽释放酶和原激肽释放酶与细胞膜的结合 将会被研究。使用纯化的前激肽释放酶，激活将是 与N-末端序列相关联，以确定如何 激活过程中一种或多种N-末端氨基酸的去除 会影响酶的活性和抗原性。亚细胞 激肽释放酶原的激活部位将通过采取 一种免疫组织化学与超声相结合的新技术 结构研究。寻找内源性组织激活 原激肽释放酶和原激肽释放酶都将继续存在。这个 原球蛋白多肽链上的活化部位和 得到的酶的N-末端序列将被表征。 N末端前肽残基的长度仍然存在于 这种激活将与肾素活性相关。这个 激肽释放酶原和原激肽释放酶激活作用的研究 关于更好地理解这两个经常相反的 可以控制正常和异常血液的作用系统 压力。

The investigations of renal enzymes and their activators will be continued with emphasis on tissue kallikrein and renin. Although these enzymes are concentrated in the kidney, they are present in other organs as well. The recent developments in deciphering the structure of pro-renin and prokallikrein make it possible to establish the mode of activation and identify endogenous activating enzymes of the inactive pro-enzymes. The activation of both homogeneous prokallikrein and prokallikrein hound to cell membranes will be studied. With purified prokallikrein, activation will be correlated with the N-terminal sequence in order to determine how the removal of one or more N-terminal amino acids during activation could affect enzymatic activity and antigenicity. The subcellular site of activation of prokallikrein will be localized by adopting a novel technique combining immunohistochemistry with ultra- structural studies. The search for endogenous tissue activating enzymes for both prokallikrein and prorenin will continue. The site of activation in the peptide chain of prorenin and the resulting N-terminal sequence of the enzyme will be characterized. The length of the N-terminal propeptide residue still present after the activation will be correlated with the renin activity. The studies on the activation of prokallikrein and prorenin will bring about a better understanding of the two frequently oppositely acting systems, which can control normal and abnormal blood pressure.