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Purification and properties of aminoaldehyde dehydrogenase fromAvenasativa

โœ Scribed by Jeyanthi Livingstone; Izumi Yoshida; Yutaka Tarui; Kiyoo Hirooka; Yoshihiro Yamamoto; Nobuo Tsutui; Eiji Hirasawa

Book ID
106302294
Publisher
Springer
Year
2002
Tongue
English
Weight
154 KB
Volume
115
Category
Article
ISSN
0918-9440

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โœ Dr. A. C. Schwartz; A. E. Krause ๐Ÿ“‚ Article ๐Ÿ“… 2007 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 780 KB

## Abstract NADH dehydrogenase (E.C. 1.6.99.3) was purified thirtyfold from the soluble proteins of the anaerobic __Propionibacterium shermanii.__ The identity of the soluble enzyme with the NADH dehydrogenase bound to the particle fraction obtained from ultracentrifugation at 105000 ยท g for 3 hrs