Purification and characterization of a membrane-bound protein kinase from human erythrocytes.
Open Access
- 1 March 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (6) , 2563-2568
- https://doi.org/10.1016/s0021-9258(19)85929-x
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Phosphorylation and dephosphorylation of spectrinJournal of Supramolecular Structure, 1978
- Selective phosphorylation of erythrocyte membrane proteins by the solubilized membrane protein kinasesBiochemistry, 1977
- On the mechanism of ATP-induced shape changes in the human erythrocyte membranes: the role of ATPThe Journal of cell biology, 1977
- On the mechanism of ATP-induced shape changes in human erythrocyte membranes. I. The role of the spectrin complex.The Journal of cell biology, 1977
- Physico-chemical characterization of the spectrin tetramer from bovine erythrocyte membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- An analysis of the autophosphorylation of rabbit and human erythrocyte membranesBiochemistry, 1976
- Phosphorylation of endogenous substrates by erythrocyte membrane protein kinases. I. Monovalent cation-stimulated reactionBiochemistry, 1974
- Phosphorylation of endogenous substrates by erythrocyte membrane protein kinases. II. Cyclic adenosine monophosphate-stimulated reactionsBiochemistry, 1974
- Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergentsJournal of Supramolecular Structure, 1973