A rapid method for the purification of octopine dehydrogenase for the determination of cell metabolites |
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| Authors: | G Gäde E J H Head |
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| Institution: | (1) N.E.R.C. Unit of Marine Invertebrate Biology, Marine Science Laboratories, Menai Bridge, Gwynedd, UK;(2) Present address: Institut für Zoophysiologie, AVZ I, Rheinische Friedrich-Wilhelms-Universität, Endenicher Allee 11-13, D-5300 Bonn, Federal Republic of Germany |
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| Abstract: | Summary Unlike other NAD+-dependent dehydrogenases, octopine dehydrogenase was not bound by blue Sepharose. A rapid 2-step purification procedure (gel filtration on Sephadex G-100 followed by affinity chromatography on blue Sepharose) resulted in a final preparation of octopine dehydrogenase which had a sp. act. of 65 units/mg protein and was free of contaminating NAD+-oxidoreductases. This preparation has been used successfully for the estimation of phospho-L-arginine, L-arginine and octopine in perchloric acid extracts.Supported by a grant from the Deutsche Forschungsgemeinschaft (Ga 241/1). |
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