The solubilization and gel electrophoresis of membrane enzymes by use of detergents

The solubilization and electrophoresis of membrane proteins with phenol and acetic acid or urea usually have deleterious effects on enzyme activities. A method is reported of solubilizing rat-liver plasma membrane proteins, by the use of the detergents sodium dodecyl sulfate, sodium deoxycholate, and Triton X-100, for subsequent electrophoresis of the enzymes on 7% polyacrylamide gel. An important feature of the method is the incorporation of detergent into the gel and the electrophoresis buffer. By use of this procedure, non-specific esterases, an alkaline phosphatase, and alkaline phosphodiesterase are detectable on the gels. The method is compared with other techniques currently being used, and it would appear that this method will have general usefulness in the study of membrane enzymes.