An experiment eliminating the rotating carrier mechanism for the active transport of Ca ion in sarcoplasmic reticulum membranes.

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Abstract
The rotating carrier mechanism of the translocation event in membrane transport was studied. To the Ca-ATPase in intact rabbit skeletal muscle sarcoplasmic reticulum membranes, 2,4-[3H]dinitrophenyl-cadaverin was covalently attached by the action of the enzyme, transglutaminase. The binding of anti-2,4-dinitrophenyl antibodies to the 2,4-dinitrophenyl-modified membranes had no effect on either the Ca-ATPase activity or the Ca2+ transport rate of the membranes. The results rule out the rotating carrier mechanism in this system. A different scheme for the translocation process, the aggregate rearrangement mechanism, is discussed.