Purification and characterization of the Ca2+-ATPase of plasma membranes from Ehrlich ascites mammary carcinoma cells
| Autor: | Reinhard Wetzker, Reinhard Klinger, Frank-D. Böhmer, Elke Müller, Michael Scheven, Holger Hegewald, Richard Grosse |
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| Rok vydání: | 1986 |
| Předmět: |
Calmodulin
ATPase Biophysics Calcium-Transporting ATPases Biochemistry Chromatography Affinity Ehrlich ascites carcinoma chemistry.chemical_compound Affinity chromatography Animals Phosphorylation Carcinoma Ehrlich Tumor chemistry.chemical_classification Molecular mass biology Cell Membrane Erythrocyte Membrane Vanadium Cell Biology Chromatography Ion Exchange Enzyme Activation EGTA Kinetics Membrane Enzyme chemistry biology.protein Calcium Calmodulin-Binding Proteins Electrophoresis Polyacrylamide Gel Vanadates |
| Zdroj: | Biochimica et biophysica acta. 854(1) |
| ISSN: | 0006-3002 |
| Popis: | Ca2+-ATPase was isolated from plasma membranes of Ehrlich ascites mammary carcinoma cells by means of calmodulin affinity chromatography. The purification procedure included removal of endogenous calmodulin from a Triton X-100 solubilizate of the membranes by DEAE ion-exchange chromatography as an essential step. With respect to its molecular mass, activation by calmodulin, Ca2+-dependent phosphorylation and highly sensitive inhibition by orthovanadate, the purified enzyme resembles the Ca2+-ATPase of erythrocyte membranes. In contrast to the strong calmodulin dependence of the isolated enzyme the Ca2+-ATPase in native Ehrlich ascites carcinoma cell membranes cannot be remarkably stimulated by added calmodulin. It is suggested that the membrane-bound Ca2+-ATPase in the presence of Ca2+ is activated by interaction with endogenously bound calmodulin. |
| Databáze: | OpenAIRE |
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