[Solubilization and reconstruction of microsomal AMP-deaminase from skeletal muscles].
Microsomal AMP-deaminase was solubilized by 0.5 M KCl after treatment of microsomal membranes with 0.12 M KCl. Using disc-electrophoresis in polyacrylamide gel in the presence of sodium dodecyl sulfate one major protein component (mol. weight about 90 000) and three minor ones with molecular weights of 110 000, 80 000, and 60 000 were found in the soluble fraction. In addition to proteins, the fraction was found in the soluble fraction. In addition to proteins, the fraction was found to contain a small amount of phospholipids. The deaminase found in the solution may be reconstructed into the membranes at a decrease in KCl concentration, part of enzyme being bound in the inactive form under excess of the soluble fraction. Deaminase binding to the membranes is unaffected by the changes within the pH range of 6.2--7.8 and temperature range of 4--10 degrees C. It is assumed that AMP-deaminase is bound to other membrane components by electrostatic bonds.
[Solubilization and reconstruction of microsomal AMP-deaminase from skeletal muscles]. Microsomal AMP-deaminase was solubilized by 0.5 M KCl after treatment of microsomal membranes with 0.12 M KCl. Using disc-electrophoresis in polyacrylamide gel in the presence of sodium dodecyl sulfate one major protein component (mol. weight about 90 000) and three minor ones with molecular weights of 110 000, 80 000, and 60 000 were found in the soluble fraction. In addition to proteins, the fraction was found in the soluble fraction. In addition to proteins, the fraction was found to contain a small amount of phospholipids. The deaminase found in the solution may be reconstructed into the membranes at a decrease in KCl concentration, part of enzyme being bound in the inactive form under excess of the soluble fraction. Deaminase binding to the membranes is unaffected by the changes within the pH range of 6.2--7.8 and temperature range of 4--10 degrees C. It is assumed that AMP-deaminase is bound to other membrane components by electrostatic bonds.