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Partial purification and properties of octopine dehydrogenase and the formation of octopine inAnodonta cygnea L.

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Summary

  1. 1.

    Octopine dehydrogenase was purified 120-fold from adductor muscle of the fresh water bivalveAnodonta cygnea L. by gel filtration on Sephadex G-100 and chromatography on DEAE-Sephadex A 50 and hydroxylapatite.

  2. 2.

    In comparison to the purified enzyme from marine species the final preparation of the octopine dehydrogenase fromAnodonta showed similarK m (1.0 mM for arginine, 0.4 mM for pyruvate, 1.2 mM for octopine) and pH values (6.3 and 10.1 respectively) and a similar molecular weight (40 000 Dalton).

  3. 3.

    During electrophoresis on standard polyacrylamide gels octopine dehydrogenase showed a multiple band pattern which is due to isoenzymes.

  4. 4.

    Alanine, lactate and succinate had no effect on the enzyme activity. Octopine, however, inhibited it strongly (Fig. 4)

  5. 5.

    Thede-novo synthesis of octopine in isolated adductor muscles from14C-pyruvate was not significantly different under aerobic or anaerobic conditions.

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Abbreviations

DTT:

dithiothreitol

EDTA:

ethylene diamine tetraacetic acid

NBT:

nitro blue tetrazolium

PMS:

phenazine methosulphate

TRA:

triethanolamine

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Author notes

  1. Gerd Gäde

    Present address: Laboratory of Chemical Animal Physiology, State University of Utrecht, 8, Padualaan-Transitorium III, Utrecht, The Netherlands

Authors and Affiliations

  1. Lehrstuhl für Tierphysiologie, Zoologisches Institut der Westfälischen Wilhelms-Universität, Münster, Federal Republic of Germany

    Gerd Gäde & Manfred Grieshaber

Authors
  1. Gerd Gäde
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  2. Manfred Grieshaber
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Gäde, G., Grieshaber, M. Partial purification and properties of octopine dehydrogenase and the formation of octopine inAnodonta cygnea L.. J Comp Physiol B 102, 149–158 (1975). https://doi.org/10.1007/BF00691300

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  • DOI: https://doi.org/10.1007/BF00691300

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