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Purification and characteristics of glutamate dehydrogenase (GDH) from triticale roots

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Abstract

In the investigated 14 day old triticale seedlings a much higher GDH activity was observed in roots than in leaves. The enzyme from the roots was purified up to the state of homogeneity (about 400 fold). The purified enzyme showed a higher activity in the presence of reduced coenzyme forms (NAD(P)H) than their oxidated forms. In the presence of NAD(P)H the enzyme showed absolute specificity to 2-oxoglutarate and in cooperation with NAD(P)+ to L-glutamate. The Km values determined for particular substrates indicate a high affinity of NADPH-GDH to ammonium ions.

Optimum pH, temperature and thermostability of GDH depended on the type and form of the coenzyme. Molecular mass of purified enzyme was 257 kDa. It seems that native GDH is composed of six identical subunits of the molecular mass 42.5 kDa.

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Authors and Affiliations

  1. Department of Biochemistry, Warsaw Agricultural University, 02-528, Warszawa, 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. Purification and characteristics of glutamate dehydrogenase (GDH) from triticale roots. Acta Physiol Plant 23, 399–405 (2001). https://doi.org/10.1007/s11738-001-0049-2

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  • DOI: https://doi.org/10.1007/s11738-001-0049-2

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