肠激酶 来源于猪肠

来自Sigma的酶被用来激活酶原，以检测胰蛋白酶的活性。研究胰蛋白酶原中未配对半胱氨酸的结构和进化结果。该产品已用于测量胰蛋白酶，同时研究农药诱导的基因表达改变在美洲螯龙虾中的影响。Sigma的酶已用于开发一种新的测定方法，在脂结合apoA-I存在的情况下，测量无脂apoA-I的水平。肠肽酶可以特异性切割人的无脂apoA-I，但不能切割apoA-I的脂质结合形式，从而产生22 kDa的N端片段。还用它研究了钙和植酸对胰蛋白酶原激活和胰蛋白酶稳定性的影响。来自猪肠的肠激酶已用于研究大鼠肠肽酶的互补DNA克隆和测序。来自猪肠的肠激酶也用于了解胃抑制多肽的胰岛素性区域。 Enterokinase from porcine intestine has been used in a study to investigate complementary DNA cloning and sequencing of rat enteropeptidase. Enterokinase from porcine intestine has also been used to learn more about the insulinotropic region of the gastric inhibitory polypeptide. The enzyme from Sigma has been used to activate zymogens in order to detect trypsin activity. The study to investigated the structural and evolutionary consequences of unpaired cysteines in trypsinogen. The product has been used to measure trypsin while studying the effect of pesticide induced alterations in gene expression in the lobster, Homarus americanus The enzyme from Sigma has been used to develop a novel assay for measuring levels of lipid-free apoA-I in the presence of lipid-bound apoA-I. Enteropeptidase can specifically cleave human lipid-free apoA-I but not its lipid-bound form resulting in an N-terminal fragment of 22 kDa. It has also been used in a study to examine the effect of calcium and phytic acid on the activation of trypsinogen and the stability of trypsin.

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