An experiment eliminating the rotating carrier mechanism for the active transport of Ca ion in sarcoplasmic reticulum membranes.
An experiment has been carried out to test the rotating carrier mechanism of the translocation event in membrane transport. To the Ca-ATPase in intact sarcoplasmic reticulum membranes, 2,4-[3H]dinitrophenyl-cadaverine has been covalently attached by the action of the enzyme, transglutaminase. The binding of anti-2,4-dinitrophenyl antibodies to the 2,4-dinitrophenyl-modified membranes was found to have no effect on either the Ca-ATPase activity or the Ca ion transport rate of the membranes. These results rule out the rotating carrier mechanism in this system. A different scheme for the translocation process, the aggregate rearrangement mechanism, is discussed.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D000937:Antigen-Antibody Reactions; D001693:Biological Transport, Active; D002118:Calcium / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D008954:Models, Biological; D009124:Muscle Proteins; D009578:Nitrobenzenes / Q000276:immunology; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D009124:Muscle Proteins; D009578:Nitrobenzenes; D000251:Adenosine Triphosphatases; D002118:Calcium