Ca2+/Mg2+-Dependent ATPase in Sarcoplasmic Reticulum

Kinetic Properties in Its Monomeric and Oligomeric Forms
  • Taibo Yamamoto
  • Yuji Tonomura


Since Hasselbach and Makinose (1961) showed the existence of the Ca2+/Mg2+-dependent ATPase in the membrane of isolated sarcoplasmic reticulum (SR), considerable progress has been made concerning the mechanism of the active transport of Ca2+. The outline of the transport mechanism, which has been obtained mainly from kinetic studies of the Ca2+/Mg2+-dependent ATPase, is described briefly as follows: 1 mole of ATP and 2 moles of Ca2+ bind to 1 mole of the membrane-bound ATPase on the outside of the SR vesicle. The terminal phosphate of ATP is transferred to an aspartyl residue of the enzyme to form a phosphoenzyme. At the same time, Ca2+ is translocated from outside to inside the membrane. The phosphoenzyme is then hydrolyzed in the presence of Mg2+. The entire process of Ca2+ transport can be reversed. When SR vesicles loaded with Ca2+ are reacted with P i in the presence of Mg2+ and EGTA, 1 mole of phosphoenzyme is formed. When ADP is added to the phosphoenzymes, 2 moles of Ca2+ are released accompanying the formation of 1 mole of ATP. These studies have been reviewed in detail by Hasselbach (1979), Inesi (1979), Martonosi (1975), Tada et al. (1978), and Yamamoto et al. (1979).


Sarcoplasmic Reticulum Dependent ATPase Terminal Phosphate Sarcoplasmic Reticulum Membrane Sarcoplasmic Reticulum Vesicle 
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Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Taibo Yamamoto
    • 1
  • Yuji Tonomura
    • 1
  1. 1.Department of Biology, Faculty of ScienceOsaka UniversityToyonaka, Osaka 560Japan

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