Purification and properties of poly(ADP-ribose) synthetase from mouse testicle |
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| Authors: | M Agemori H Kagamiyama M Nishikimi Y Shizuta |
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| Affiliation: | 1. Department of Medical Chemistry, Kochi Medical School, Kochi 781-51, India;2. Department of Medical Chemistry, Osaka Medical College, Osaka 569, Japan |
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| Abstract: | Poly(ADP-ribose) synthetase has been purified to apparent homogeneity from mouse testicle by a rapid and simple procedure using column chromatography on DNA-agarose and on Cibacron blue F3G-A-Sephadex G-150. The purified enzyme absolutely requires DNA for activity, and half-maximal activation occurs at a DNA concentration of 25 μg/ml. The Km for NAD and V at pH 8.0 and 25 °C are 47 μm and 1400 nmol/min/ mg, respectively. The molecular weight is 116,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino acid analysis indicates that the mouse testicle enzyme is very similar to calf thymus enzyme, but there is a difference in the contents of several amino acid residues between the two enzymes. This difference appears to reflect species or tissue specificity of poly(ADP-ribose) synthetase. |
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| Keywords: | Author to whom all correspondence should be addressed. |
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