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The sulphydryl groups of ox brain and liver glutamate dehydrogenase preparations and the effects of oxidation on their inhibitor sensitivities

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Abstract

Glutamate dehydrogenase preparations from several sources have been shown to have suffered limited proteolysis during purification. This proteolysis has been previously shown to involve removal of the N-terminal tetrapeptide and to result in changes in the regulatory properties of the enzyme. In the present work the previously unidentified N-terminal residue of the unproteolysed enzyme from ox brain and liver is shown to be cysteine. The thiol group of this residue is masked in the native enzyme but it becomes accessible after reduction. Exposure of solutions of the unproteolysed enzyme to air oxidation causes large changes in its sensitivity to inhibition by the antipsychotic drug perphenazine, GTP and by high concentrations of NADH. No such changes occurred in the behaviour of preparations of the enzyme that had suffered proteolysis during purification under these conditions.

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Author notes

  1. Ivan Couée

    Present address: Station de Physiologie Vegetale, INRA Centre de Recherche Bordeaux, BP 81, 33883, Villenave d'Ornon Cedex, France

Authors and Affiliations

  1. Department of Biochemistry, Trinity College, Dublin 2, Ireland

    Ivan Couée & Keith F. Tipton

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  1. Ivan Couée
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Special issue dedicated to Dr. Santiago Grisolia.

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Couée, I., Tipton, K.F. The sulphydryl groups of ox brain and liver glutamate dehydrogenase preparations and the effects of oxidation on their inhibitor sensitivities. Neurochem Res 16, 773–780 (1991). https://doi.org/10.1007/BF00965686

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