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Biospecific Affinity Chromatographic Purification of Octopine Dehydrogenase from Molluscs

✍ Scribed by Patricia Mulcahy; Tadhg Griffin; Padraig O'Carra

Book ID
115645098
Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
161 KB
Volume
9
Category
Article
ISSN
1046-5928

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Purification and characterisation of oct
Purification and characterisation of octopine dehydrogenase from the marine nemerteanCerebratulus lacteus(Anopla: Heteronemerta): comparison with scallop octopine dehydrogenase
✍ G. GΓ€de; K. -H. Carlsson πŸ“‚ Article πŸ“… 1984 πŸ› Springer-Verlag 🌐 English βš– 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