Purification and characterisation of oct
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G. Gäde; K. -H. Carlsson
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Article
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1984
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Springer-Verlag
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English
⚖ 864 KB
Octopine dehydrogenase from the nemertean Cerebratulus lacWus was purified over 1 000-fold to almost homogeneity. The enzyme does not bind to arginine Sepharose 4B. It has a monomeric structure with a relative molecular mass of 40 000. Two isoenzymes were identified with isoelectric points of 5.6 an