Gennis R B, Strominger J L
J Biol Chem. 1976 Mar 10;251(5):1277-82.
The activation of kinase by neutral detergents has been examined. Of those detergents tested, only those with short chain and unsaturated chain hydrophobes were successful activators at 25 degrees. In addition to these structural requirements, a dependence upon hydrophilic-lipophilic balance number was observed when mixing hydrophobic and hydrophilic detergents. Most pairs tested showed an optimal hydrophilic-lipophilic balance number for kinase activation in the hydrophobic range of 6 to 9. Thus, there appears to be both a structural and a relative hydrophobic requirement for activation, and hydrophilic-lipophilic balance number may be a measure of the physical properties of the lipid required for activation.
已对中性去污剂对激酶的激活作用进行了研究。在测试的那些去污剂中，只有具有短链和不饱和链疏水基团的去污剂在25摄氏度时是成功的激活剂。除了这些结构要求外，在混合疏水和亲水去污剂时，还观察到对亲水亲油平衡值的依赖性。大多数测试的组合在6至9的疏水范围内显示出激酶激活的最佳亲水亲油平衡值。因此，激活似乎存在结构和相对疏水要求，亲水亲油平衡值可能是激活所需脂质物理性质的一种度量。
