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Effect of selected compounds on the activity of glutamate dehydrogenase from triticale roots

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Abstract

The influence of selected factors on the activity of highly purified GDH in triticale roots was investigated in vitro. In the presence of 2-ME, NADH-GDH activity increased by 400 %, while NADPH-GDH activity rose by 500 %. No effect of reducing factors on NAD(P)+-GDH reaction was detected. The sulphydryl groups inhibitors, such as p-chloromercuribenzoate (p-CMB) and iodoacetamide, proved the strongest inhibitors of the aminative reaction. Metal-binding compounds: ethylenediaminetetraacetic acid disodium salt (EDTA) and Zinkov also considerably inhibited NAD(P)H-GDH activity. Diisopropylfluorophosphate (DFP) and pepstatin A, the inhibitors specific for -OH serine and COO− aspartic acid groups respectively, caused a non-significant NAD(P)H-GDH activity decrease. Cd2+, Co2+, Hg2+, Mg2+, Pb2+ and Zn2+ ions strongly inhibited the amination reaction, whereas their inhibiting effect upon NAD+-GDH activity was negligible. Among the applied ions, only Ca2+ activated NADH-GDH.

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Abbreviations

p-CMB:

p-chloromercuribenzoate

DFP:

diiopropylfluorophosphate

EDTA:

ethylenediaminetetraacetic acid disodium salt

2-ME:

2-mercaptoethanol

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Authors and Affiliations

  1. Department of Biochemistry, Warsaw Agricultural University, 02-528 Warszawa, Rakowiecka 26/30, Poland

    J. Kwinta, K. Bartoszewicz & W. Bielawski

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  1. J. Kwinta
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  2. K. Bartoszewicz
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  3. W. Bielawski
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Kwinta, J., Bartoszewicz, K. & Bielawski, W. Effect of selected compounds on the activity of glutamate dehydrogenase from triticale roots. Acta Physiol Plant 24, 279–283 (2002). https://doi.org/10.1007/s11738-002-0052-2

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  • DOI: https://doi.org/10.1007/s11738-002-0052-2

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