Bancells L, Balsa D, Gómez N, Unzeta M
Biochem Pharmacol. 1987 Aug 1;36(15):2539-46. doi: 10.1016/0006-2952(87)90528-4.
It has been reported that monoamine oxidase (MAO) activity (EC1.4.3.4) and, in general, enzymes possessing cationic substrates, were activated and inhibited by anionic and cationic detergents, respectively. In order to examine this hypothesis, the effect of the zwitterionic detergent CHAPS 3-[(3-cholamido propyl) dimethyl ammonio]-1-propanesulphonate was studied in comparison with the effects of cationic, anionic, and non-ionic detergents. The non-denaturating zwitterionic detergent CHAPS was used to solubilise rat liver monoamine oxidase MAO (EC1.4.3.4) of mitochondrial and microsomal origin; the solubilisation conditions, purification, inhibition and kinetic studies were then determined. These results are compared with those previously obtained with the non-ionic detergent Triton X-100, which would also be expected to have no net charge, and are interpreted in terms of specific ionic effects.
据报道,单胺氧化酶(MAO)活性(EC1.4.3.4),以及一般而言具有阳离子底物的酶,分别被阴离子和阳离子去污剂激活和抑制。为了检验这一假设,研究了两性离子去污剂3-[(3-胆酰胺丙基)二甲基铵]-1-丙烷磺酸盐(CHAPS)的作用,并与阳离子、阴离子和非离子去污剂的作用进行了比较。使用非变性两性离子去污剂CHAPS来溶解大鼠肝脏线粒体和微粒体来源的单胺氧化酶MAO(EC1.4.3.4);然后确定溶解条件、纯化、抑制和动力学研究。将这些结果与先前用非离子去污剂Triton X-100获得的结果进行比较,Triton X-100预计也没有净电荷,并根据特定的离子效应进行解释。