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Amino acid analysis, electron resonance spectroscopy, metal analysis, and analysis for subunit structure have been performed on bovine superoxide dismutase. The enzyme consists of two subunits of identical molecular weight held together by disulfide bonds. Superoxide dismutase has been purified from bovine heart by a procedure which was previously developed for the isolation of this enzyme from bovine erythrocytes. The heart enzyme is judged to be identical with the erythrocyte enzyme on the basis of response to an unusual purification procedure, specific enzymatic activity, content of copper and zinc, molecular weight, amino acid composition, ultraviolet absorption spectrum, and electron paramagnetic resonance spectrum. The widespread distribution of superoxide dismutase in mammalian tissues is taken as one indication of its importance to the survival of the cells which constitute these diverse tissues.
Keele et al. (Sat,) studied this question.
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