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Isolation of ADP-ribosyltransferase by affinity chromatography

โœ Scribed by Helmut J. Burtscher; Bernhard Auer; Helmut Klocker; Manfred Schweiger; Monica Hirsch-Kauffmann

Publisher
Elsevier Science
Year
1986
Tongue
English
Weight
583 KB
Volume
152
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

An affinity adsorbent for ADP-ribosyltransferase (EC 2.4.2.30) has been synthesized by coupling 3-aminobenzamide to Sepharose 4B. Using this material, ADP-ribosyltransferase from human placenta has been purified from crude extract to homogeneity within a few hours. The enzyme has an apparent Km for NAD+ of 52 microM. Its molecular mass is 115,000 as determined by gel electrophoresis. The enzyme is DNA dependent and stimulated by histone, its temperature optimum is at 25 degrees C, and its pH optimum is around pH 9. alpha-NAD+, thymidine, caffeine, theophylline, theobromine, 3-methoxybenzamide, and nicotinamide inhibit the enzyme. Purification of ADP-ribosyltransferases from horse, rat, and chicken liver was also achieved with the method described.

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