The differential release of basal ATPase, Ca2+-dependent ATPase, 5'-nucleotidase and cholesterol during homogenization of skeletal muscle.

Abstract

The influence of homogenization times on the presence of constituents in the microsomal fraction of skeletal muscle was investigated. Membranes having Ca2+-activated ATPase activity have a fragmentation pattern distinct from that of membranes displaying Ca2+-independent or basal ATPase activity. These latter membranes were found in highest specific concentration in the microsomal fraction prepared from homogenates subjected to short periods of homogenization. 5'-Nucleotidase (EC 3.1.3.5) activity paralleled that of basal ATPase on short periods of homogenization, as also did the specific concentration of cholesterol. Longer periods of homogenization led to a decrease in the specific activity of basal atpase, which reached its lowest value at 120s of homogenization, whereas the specific activity of 5'-nucleotidase and the specific concentration of cholesterol decreased initially in a similar manner to basal ATPase, but both increased substantially after the longest period of homogenization.