[A comparative study of the properties of ouabain-sensitive phosphatase in rat erythrocyte ghosts and spectrin-free membranes].
The removal of the membrane skeleton proteins (MSP), chiefly spectrin and actin, from the rat erythrocyte ghosts was shown to result in a decrease of both the total Na, K-ATPase activity and a partial reaction of the enzyme, namely the phosphatasic one. Besides, modulating effects of the effectors promoting the enzyme conformational transitions (ATP and Mg2+) on the ouabain-sensitive K-phosphatase is changed. For instance, a pronounced activation of the K-phosphate in a high-potassium medium in the presence of 1 mM ATP disappeared and the degree of the enzymatic activity enhancement in response to increasing MgCl2 concentrations (from 1.5 to 6 mM) is decreased. The data obtained are discussed from the viewpoint of possible involvement of the erythrocyte MSP in the catalytic of Na, K-ATPase.
Kazennov
A M
AM
Rustamov
F A
FA
Frolova
O V
OV
Shalabodov
A D
AD
D000199:Actins; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002384:Catalysis / Q000187:drug effects; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000201:enzymology*; D015636:Magnesium Chloride / Q000494:pharmacology; D008297:Male; D010042:Ouabain / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000097:blood* / Q000187:drug effects*; D011487:Protein Conformation / Q000187:drug effects; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000097:blood / Q000187:drug effects; D013049:Spectrin
D000199:Actins; D004791:Enzyme Inhibitors; D015636:Magnesium Chloride; D013049:Spectrin; D010042:Ouabain; D000255:Adenosine Triphosphate; D010744:Phosphoric Monoester Hydrolases; D000254:Sodium-Potassium-Exchanging ATPase
Sravnitel'noe izuchenie svoĭstv uabain-chuvstvitel'noĭ fosfatazy v teniakh i besspektrinovykh membranakh éritrotsitov krysy.