✦ LIBER ✦

Phosphorylation of casein by human erythrocyte membrane-bound protein kinase: competition of casein with endogenous substrates

✍ Scribed by J. D. Vickers; J. Brierley; M. P. Rathbone

Publisher: Springer
Year: 1979
Tongue: English
Weight: 800 KB
Volume: 49
Category: Article
ISSN: 0022-2631
DOI: 10.1007/bf01868721

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Phosphorylation of membrane proteins by

Phosphorylation of membrane proteins by cytosolic casein kinases in human erythrocytes. Effect of monovalent ions, 2,3-bisphosphoglycerate and spermine

✍ Giulio Clari; Vittorio Moret 📂 Article 📅 1985 🏛 Springer 🌐 English ⚖ 508 KB

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

Phosphorylation of cytosolic proteins by

Phosphorylation of cytosolic proteins by casein kinases in human erythrocytes. Response to ionic strength and to 2,3-bisphosphoglycerate

✍ Giulio Claril; Vittorio Moret 📂 Article 📅 1987 🏛 Springer 🌐 English ⚖ 504 KB

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