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
โฆ LIBER โฆ
Protein kinase nii from calf thymus chromatin. isolation, characterization and some functional properties
โ Scribed by Antonella Angiolillo; Fausto Panara; Alda Desgro; Cristina Petrelli; Glan Luigi Gianfranceschi
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 830 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0020-711X
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## Abstract The influence of pH, ionic strength and solidโliquid ratio on the nitrogen yield and functional properties of those isolates which can be produced through extractionโprecipitation procedures was studied. Two 2^3^ factorial plans were executed for the extraction in acidic and basic mediu