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Tryptophanase from Aeromonas liquefaciens. Purification molecular weight and some chemical, catalytic and immunochemical properties

โœ Scribed by James L. Cowell; Karen Moser; Ralph D. Demoss

Book ID
115733319
Publisher
Elsevier Science
Year
1973
Weight
904 KB
Volume
315
Category
Article
ISSN
0005-2744

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Tryptophanase from a marine bacterium,Vi
Tryptophanase from a marine bacterium,VibrioK-7 synthesis, purification, and some chemical catalytic properties
โœ Dixie D. Whitt; Michael J. Klug; R. D. DeMoss ๐Ÿ“‚ Article ๐Ÿ“… 1979 ๐Ÿ› Springer ๐ŸŒ English โš– 690 KB

The conditions for synthesis, purification, and properties of tryptophanase by a marine organism (Vibrio K-7) were studied. Tryptophanase was induced by tryptophan and its analogs, and partially repressed by 0.5 % glucose or glycerol. NaC1 (0.4 M) was required for optimal growth and tryptophanase ac