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.