Energy Metabolism of Various Substrates and the 2,3-Bisphosphoglycerate Bypass in Human Erythrocytes
β Scribed by Karl-Hugo QUADFLIEG; Karl BRAND
- Book ID
- 115116441
- Publisher
- John Wiley and Sons
- Year
- 1978
- Tongue
- English
- Weight
- 534 KB
- Volume
- 82
- Category
- Article
- ISSN
- 1432-1327
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The endogenous phosphorylation of human erythrocyte cytosolic proteins is markedly increased when the crude cytosol, prior to incubation in the presence of [y-32P] ATP, is submitted to DEAE-cellulose chromatography. Some proteins, including 22 and 23 kDa proteins, are preferentially phosphorylated b
Membrane proteins of human erythrocytes can be phosphorylated not only by membrane casein kinase (MS) but also by cytosolic casein kinases CS and CTS, resembling casein kinase I and II, respectively. Casein kinase CS, like membrane casein kinase MS, preferentially phosphorylates membrane proteins su