Abstract
Poly(ADPribose) synthetase has been purified to apparent homogeneity from sheep testis by a simple procedure using three chromatographic steps (DNA-agarose, blue Sephadex G-150 and phosphocellulose P11). A concentrated enzyme preparation, 3.5 mg, with a specific activity of 1265 nmol/min per mg was obtained from 250 g of tissue. DNA was absolutely required for enzyme activity. The half-maximal activation occurred at the concentrations of 11 μg/ml for highly polymerized calf thymus DNA and 2 μg/ml for sonicated calf thymus DNA. The K m for NAD was 57 μM. The molecualr weight was 120 000, determined by gel electrophoresis in the presence of sodiym dodecyle sulfate. Amino acid analysis indicated that the main amino acid species of sheep testis enzyme were very similar to those of enzymes from other sources.
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