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Characterization of the glyceraldehyde 3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis

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Abstract

Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) from the extremely halophilic archaebacterium Haloarcula vallismortis has been purified in a four step procedure to electrophoretic homogeneity. The enzyme is a tetramer with a relative molecular mass of 160000. It is strictly NAD+-dependent and exhibits its highest activity in 2 mol/l KCl at 45°C. Amino acid analysis and isoelectric focusing indicate an excess of acidic amino acids. Two parts of the primary sequence are reported. These peptides have been compared with glyceraldehyde 3-phosphate dehydrogenases from other archaebacteria, eubacteria and eucaryotes. The peptides show a high grade of similarity to glyceraldehyde 3-phosphate dehydrogenase from eucaryotes.

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Abbreviations

BCA:

bicinchoninic acid

CTAB:

cetyltrimethyl ammonium bromide

DTE:

dithioerythritol

DTT:

dithiothreitol

GAP:

glyccraldehyde 3-phosphate

GAPDH:

glyceraldehyde 3-phosphate dehydrogenase

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Authors and Affiliations

  1. Institut für Physiologische Chemie, Ruhr-Universität Bochum, Universitätsstrasse 150, W-4630, Bochum, Germany

    Birgit Prüß, Helmut E. Meyer & August W. Holldorf

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  1. Birgit Prüß
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  2. Helmut E. Meyer
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  3. August W. Holldorf
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Prüß, B., Meyer, H.E. & Holldorf, A.W. Characterization of the glyceraldehyde 3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis . Arch. Microbiol. 160, 5–11 (1993). https://doi.org/10.1007/BF00258139

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  • DOI: https://doi.org/10.1007/BF00258139

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