Isolation and properties of lipolysis inhibitory proteins from wheat germ and wheat bran
✍ Scribed by Patrick Borel; Denis Lairon; Elise Termine; Renée Grataroli; Huguette Lafont
- Publisher
- Springer US
- Year
- 1989
- Tongue
- English
- Weight
- 593 KB
- Volume
- 39
- Category
- Article
- ISSN
- 1573-9104
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A protein kinase, type NII, has been purified from wheat germ chromatin. The enzyme, which uses both ATP and GTP as phosphoryl donors, catalyzes the phosphorylation of casein, phosvitin and E. coli RNA polymerase, but not ofhistone proteins. Polypeptide bands at 46 kDa, 37 kDa and 25 kDa were estima
## Abstract Polyphenol oxidase (PPO) obtained from wheat bran catalyzed the oxidation of 4‐methyl catechol. Phenolic compounds found naturally in crude extract played role as an endogeneous substrate and activity of crude extract needed correction. Activity versus enzyme concentration gave a linear