[Ca2+ transport by the membrane-bound monomeric form of Ca-ATPase of sarcoplasmic reticulum].
Chromatography of a mixture of phospholipid and Ca-dependent ATPase of sarcoplasmic reticulum solubilized with choleate in a column with anionite results in proteolyposome formation. It was shown that dilution of ATPase with phospholipids makes it possible to reduce the concentration of ATPase in the membrane. Using the bifunctional reagent difluorodinitrobenzene it was demonstrated that reduction of the ATPase concentration in the membrane leads to the dissociation of the enzyme to monomers. It was disclosed that the monomeric form of ATPase is capable of active Ca2+ transport.
D000818:Animals; D001693:Biological Transport, Active; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002413:Cations, Divalent / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D008081:Liposomes / Q000378:metabolism; D011510:Proteolipids / Q000378:metabolism; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*
D002413:Cations, Divalent; D008081:Liposomes; D011510:Proteolipids; C020485:proteoliposomes; D000252:Calcium-Transporting ATPases; D002118:Calcium
Transport Ca2+ membranosviazannoĭ monomernoĭ formoĭ Ca-ATF-azy sarkoplazmaticheskogo retikuluma.