Abstract
Sarcoplasmic reticulum Ca 2+-ATPase solubilized in monomeric form by nonionic detergent was reacted with CrATP in the presence of 45Ca 2+. A Ca 2+-occluded complex formed, which was stable during high performance liquid chromatography in the presence of excess non-radioactive Ca 2+. The elution position corresponded to monomeric Ca 2+-ATPase. It is concluded that a single Ca 2+-ATPase polypeptide chain provides the full structural basis for Ca 2+ occlusion.
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