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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 35 (1979), S. 304-305 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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