通过吸附于磷脂囊泡对3-磷酸甘油醛脱氢酶活性的修饰
Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles.
作者信息
Wooster M S, Wrigglesworth J M
出版信息
Biochem J. 1976 Dec 1;159(3):627-31. doi: 10.1042/bj1590627.
Abstract
- The adsorption of [14C]carboxymethylated glyceraldehyde 3-phosphate dehydrogenase to negatively charged liposomes of phsphatidic acid/phosphatidylcholine (3:7, w/w) was investigated. The apparent association constant at I/2 = 60, pH 7.6, was 0.4 X 10(6)M-1. Adsorption decreased as ionic strength and pH were increased. 2. In the presence of negatively charged liposomes, the Km value for glyceraldehyde 3-phosphate of glyceraldehyde 3-phosphate dehydrogenase was increased and Vmax. decreased. In the presence of positively charged liposomes, the Km value for glyceraldehyde 3-phosphate decreased and there was no significant change in Vmax. Addition of Triton X-100 abolished the effect of both positively and negatively charged liposomes on the kinetic properties of the enzyme.
摘要
- 研究了[14C]羧甲基化甘油醛-3-磷酸脱氢酶对磷脂酸/磷脂酰胆碱（3:7，w/w）带负电荷脂质体的吸附作用。在离子强度I/2 = 60、pH 7.6条件下，表观缔合常数为0.4×10(6)M-1。随着离子强度和pH值的增加，吸附作用减弱。2. 在带负电荷脂质体存在的情况下，甘油醛-3-磷酸脱氢酶对甘油醛-3-磷酸的Km值升高，Vmax降低。在带正电荷脂质体存在的情况下，甘油醛-3-磷酸的Km值降低，Vmax没有显著变化。添加Triton X-100消除了带正电荷和带负电荷脂质体对该酶动力学性质的影响。
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