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

✍ Scribed by G�de, Gerd ;Grieshaber, Manfred


Book ID
104889327
Publisher
Springer-Verlag
Year
1975
Tongue
English
Weight
648 KB
Volume
102
Category
Article
ISSN
0174-1578

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Purification and characterisation of oct
✍ G. Gäde; K. -H. Carlsson 📂 Article 📅 1984 🏛 Springer-Verlag 🌐 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