𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Functional Link between Phosphorylation State of Membrane Proteins and Morphological Changes of Human Erythrocytes

✍ Scribed by L. Bordin; G. Clari; I. Moro; F. Dallavecchia; V. Moret

Book ID
115577049
Publisher
Elsevier Science
Year
1995
Tongue
English
Weight
855 KB
Volume
213
Category
Article
ISSN
0006-291X

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Changes in topography and function of th
Changes in topography and function of thylakoid membranes following membrane protein phosphorylation
✍ M. T. Black; P. Lee; P. Horton πŸ“‚ Article πŸ“… 1986 πŸ› Springer-Verlag 🌐 English βš– 695 KB

Changes in topography and function of pea (Pisum sativum L.) thylakoid membrane fractions following membrane protein phosphorylation have been studied. After protein phosphorylation the stromal membrane fraction had a higher chlorophyll a/b ratio, an increased content of light-harvesting chlorophyll

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 πŸ“‚ Article πŸ“… 1985 πŸ› Springer 🌐 English βš– 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