[The effect of the membrane skeleton of non-nucleated erythrocytes on the properties of transport ATPases].
Removal of spectrin and other proteins of membrane skeleton from rat erythrocyte membranes resulted in a significant loss of Na,K-ATPase and Ca-ATPase activities, and even more of respective phosphatase activities. At the same time the modulating influence of ATP and Ca2+ on the enzymes disappeared. These ATPase activities were reconstituted by addition of concentrated spectrin to spectrin-depleted membranes. The activating influence of Ca2+ on ouabain-resistant and ouabain-sensitive phosphatases in ghosts could be discovered only in the presence of ATP. The highest activities of both the phosphatases were revealed when both ATP (0.5 mM) and Ca2+ (10-30 mM) were present simultaneously in the incubation medium. These data show that the functioning of transport ATPases in non-nuclear erythrocyte membranes is related to the membrane skeleton: regulating influence of intracellular ATP and Ca2+ on enzymes seems to be realized through the proteins of the skeleton.
Kazennov
A M
AM
Maslova
M N
MN
D000199:Actins / Q000502:physiology; D000251:Adenosine Triphosphatases / Q000032:analysis / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D001692:Biological Transport; D003599:Cytoskeleton / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology*; D004910:Erythrocyte Membrane / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology*; D008565:Membrane Proteins / Q000032:analysis / Q000187:drug effects / Q000378:metabolism*; D010042:Ouabain / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis / Q000187:drug effects / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013049:Spectrin / Q000502:physiology
D000199:Actins; D008565:Membrane Proteins; D013049:Spectrin; D010042:Ouabain; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases
Vliianie membrannogo skeleta bez''iadernykh éritrotsitov na svoĭstv transportnykh ATFaz.