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Nucleic Acids Research, 1990, Vol. 18, No. 16 4691-4694
© 1990

Articles

An affinity matrix for the purification of poly(ADP-ribose) glycohydrolase

Hélène Thomassin, Myron K. Jacobson1, Jocelyne Guay2, Alain Verreault2, Nasreen Aboul-ela1, Luc Menard3 and Guy G. Poirier2

Centre de Recherche en Cancérologie de I'Université Laval, Hôtel-Dieu de Québec 11, Côte du Palais, Québec G1R 2J6, Canada 1Departments of Biochemistry and Medicine, Texas College of Osteopathic Medicine, University of North Texas Fort Worth, TX 76107, USA 2Laboratoire du métabolisme du poly(ADP-ribose), Endocrinologie Moléculaire, Centre Hospitalier de I'Universite Laval 2705 boul. Laurier, Sainte-Foy, Québec G1V 4G2, Canada 3Unité de Rhumatologie et d'lmmunologie, Centre Hospitalier de I'Université Laval 2705 boul. Laurier, Sainte-Foy, Québec G1V 4G2, Canada

Received June 12, 1990. Revised July 23, 1990. Accepted July 23, 1990.

The preparation of quantities of poly(ADP-ribose) glycohydrolase sufficient for detailed structural and enzymatic characterizations has been difficult due to the very low tissue content of the enzyme and its lability in late stages of purification. To date, the only purification of this enzyme to apparent homogeneity has involved a procedure requiring 6 column chromatographic steps. Described here is the preparation of an affinity matrix which consists of ADP-ribose polymers bound to dihydroxyboronyl sepharose.An application is described for the purification of poly(ADP-ribose) glycohydrolase from calf thymus inwhich a single rapid affinity step was used to replace 3 column chromatographic steps yielding enzyme of greater than 90% purity with a 3 fold increase in yield. This matrix should also prove useful for other studies of ADP-ribose polymer metabolism and related clinical conditions.


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