[Activity and electrophoretic multiplicity of molecular forms of superoxide dismutase in the formed elements of human blood].

When calculated per protein content the level of super-oxide dismutase (SOD) activity in various human blood cells proved to decrease as follows: platelet greater than erythrocyte greater than greater than lymphocyte greater than granulocyte. During gel electrophoresis of granulocyte, lymphocyte and platelet homogenates three zones of SOD activity were revealed. Two enzyme fractions disappearing after the cyanide treatment were found in the erythrocyte lysates after the removal of hemoglobin. Of the two SOD fractions of platelets, lymphocytes, and granulocytes rapidly migrating to the anode, by the capacity to be inhibited with cyanide or organic solvents the first SOD fraction was attributed to cytosol enzyme, while the second one -- to mitochondrial enzyme. The third cathode fraction was not identified. The functional role of SOD in specialized blood cells and the causes of the enzyme heterogeneity are discussed.