An Affinity Matrix for the Purification of Poly(ADP-ribose) Glycohydrolase

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1990 Aug 25

PMID 2395636

Citations 8

Authors

H Thomassin

M K Jacobson

J Guay

A Verreault

N Aboul-Ela

L Menard

G G Poirier

Affiliations

Soon will be listed here.

Abstract

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 in which 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.

Citing Articles

Poly(ADP-ribosylation) is present in murine sciatic nerve fibers and is altered in a Charcot-Marie-Tooth-1E neurodegenerative model.

Lafon Hughes L, Romeo Cardeillac C, Cal Castillo K, Vilchez Larrea S, Sotelo Sosa J, Folle Ungo G PeerJ. 2017; 5:e3318.

PMID: 28503382 PMC: 5428328. DOI: 10.7717/peerj.3318.

Regulation of poly(ADP-ribose) polymerase-1 (PARP-1) gene expression through the post-translational modification of Sp1: a nuclear target protein of PARP-1.

Zaniolo K, Desnoyers S, Leclerc S, Guerin S BMC Mol Biol. 2007; 8:96.

PMID: 17961220 PMC: 2175517. DOI: 10.1186/1471-2199-8-96.

Spatial and functional relationship between poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in the brain.

Poitras M, Koh D, Yu S, Andrabi S, Mandir A, Poirier G Neuroscience. 2007; 148(1):198-211.

PMID: 17640816 PMC: 2000859. DOI: 10.1016/j.neuroscience.2007.04.062.

Poly(ADP-ribose) turnover in quail myoblast cells: relation between the polymer level and its catabolism by glycohydrolase.

Affar E, Shah R, Poirier G Mol Cell Biochem. 1999; 193(1-2):127-35.

PMID: 10331649

Molecular heterogeneity and regulation of poly(ADP-ribose) glycohydrolase.

Ame J, Jacobson E, Jacobson M Mol Cell Biochem. 1999; 193(1-2):75-81.

PMID: 10331641

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