Abstract
Summary
The range of succinoxydase activity in whole homogenates of human liver is 150 to 200 Qo2/N. The requirements for added cytochrome c are high in spite of a known low concentration of endogenous cytochrome c, suggesting a more efficient spatial chemical organization within the intact cells of larger animals. The distribution of succinoxidase in subcellular particles is shown. The requirements for optimum succinoxidase activity are indicated and it is demonstrated that the activity is more than doubled when optimum concentrations of flask contents are used as compared with concentrations originally developed for small animal tissue homogenates. Succinoxidase is a good enzymatic identification for mitochondria in studies on the chemistry and enzymatic activity of human liver cell fractions.
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