O'Connor C J, Wallace R G
FEBS Lett. 1984 May 21;170(2):375-7. doi: 10.1016/0014-5793(84)81347-2.
Stimulation of human milk lipase by deoxycholate and its taurine and glycine conjugates was demonstrated by measuring the esterolysis reaction of 4-nitrophenylacetate. The steroidal surfactants did not bind strongly to the polar substrate but they did bind effectively to a hydrophobic site on the enzyme and these bile salt-enzyme complexes were effective catalysts. These results are compared with those for stimulation of the enzyme by cholate surfactants and it has been demonstrated that the absence of a 7 alpha-OH substituent on the steroid nucleus does not prevent stimulation of either the esterolytic or lipolytic activity of the enzyme.
通过测量对硝基苯乙酸的酯解反应,证实了脱氧胆酸盐及其牛磺酸和甘氨酸共轭物对人乳脂肪酶的刺激作用。甾体表面活性剂不会与极性底物强烈结合,但它们确实能有效地结合到酶上的一个疏水位点,并且这些胆汁盐 - 酶复合物是有效的催化剂。将这些结果与胆酸盐表面活性剂对该酶的刺激结果进行了比较,结果表明甾体核上不存在7α - 羟基取代基并不妨碍对该酶酯解或脂解活性的刺激。