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胆汁和胆汁酸对胰蛋白酶原自催化激活为胰蛋白酶的增强作用。

Enhancement of the autocatalytic activation of trypsinogen to trypsin by bile and bile acids.

作者信息

Sarkany R P, Moreland B H

出版信息

Biochim Biophys Acta. 1985 May 8;839(3):262-7. doi: 10.1016/0304-4165(85)90007-8.

Abstract

The activation of trypsinogen to trypsin in the small intestine can occur by the action of enterokinase or, alternatively, as an autocatalytic process catalysed by trypsin itself. We have found that bile salts and human bile cause a significant enhancement of the autocatalytic activation of trypsinogen. This effect is dependent on the calcium ion concentration and is most marked around pH 5.4 and 7.8. An optimum concentration exists for each bile salt at which the greatest enhancement occurs. At this concentration, certain bile salts have been shown to produce activation effects of up to 55-fold. It is suggested that this activation of the autocatalytic process by bile plays an important role in protein digestion in the small intestine, since it has been shown previously that duodenal trypsin levels are abnormally low in patients with an impairment of bile secretion.

摘要

胰蛋白酶原在小肠中被激活成为胰蛋白酶,这一过程可通过肠激酶的作用发生,或者作为由胰蛋白酶自身催化的自催化过程发生。我们发现,胆盐和人胆汁会显著增强胰蛋白酶原的自催化激活作用。这种效应取决于钙离子浓度,在pH 5.4和7.8左右最为明显。每种胆盐都存在一个最佳浓度,在该浓度下增强作用最为显著。在这个浓度下,某些胆盐已被证明能产生高达55倍的激活作用。有人认为,胆汁对自催化过程的这种激活在小肠蛋白质消化中起重要作用,因为此前已表明,胆汁分泌受损患者的十二指肠胰蛋白酶水平异常低。

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