Rinderknecht H, Nagaraja M R, Adham N F
Am J Dig Dis. 1978 Apr;23(4):332-6. doi: 10.1007/BF01072416.
Bile acids increase the release of human enteropeptidase as well as other brush-border enzymes (alkaline phosphatase, leucine aminopeptidase) from duodenal mucosa, as had been shown earlier in experimental animals. The action of bile acids is independent of their known enhancing effect on enteropeptidase activity. The pH of duodenal juice is an important, hitherto unrecognized, factor in the release mechanism of brush-border enzymes. All of the above enzymes tested were released to a markedly greater extent at pH 8.2 than 6.3, regardless of the presence or absence of bile acid. Contrary to some results obtained with animal tissue, by other investigators, our experiments with human duodenal mucosa indicate that enteropeptidase, under all conditions tested, is released at a rate considerably greater than that for alkaline phosphatase or leucine aminopeptidase. The looser association of enteropeptidase with cellular components relative to that of other brush-border enzymes, as indicated by our observations, may be related to the unique function of enteropeptidase as the trigger enzyme of protein digestion.
正如早期在实验动物中所显示的那样，胆汁酸可增加十二指肠黏膜中人类肠肽酶以及其他刷状缘酶（碱性磷酸酶、亮氨酸氨肽酶）的释放。胆汁酸的作用与其已知的增强肠肽酶活性的作用无关。十二指肠液的pH值是刷状缘酶释放机制中的一个重要但迄今未被认识到的因素。无论有无胆汁酸，所有上述测试的酶在pH 8.2时的释放程度都明显大于pH 6.3时。与其他研究者在动物组织上获得的一些结果相反，我们用人十二指肠黏膜进行的实验表明，在所有测试条件下，肠肽酶的释放速率都比碱性磷酸酶或亮氨酸氨肽酶的释放速率大得多。我们的观察表明，相对于其他刷状缘酶，肠肽酶与细胞成分的结合较松散，这可能与肠肽酶作为蛋白质消化触发酶的独特功能有关。
