Ca2+-binding properties of a unique ATPase inhibitor protein isolated from mitochondria of bovine heart and rat skeletal muscle.

Abstract

Previous studies showed that Ca2+ induced monomer to active dimer interconversion of a mitochondrial ATPase inhibitor protein from bovine heart or rat skeletal muscle (Yamada, E.W., Huzel, N.J. and Dickison, J.C. (1981) J. Biol. Chem. 256, 10203-10207). Initial equilibrium dialysis measurements of Ca2+ binding showed that this unique protein possesses three… (More)

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@article{Yamada1985Ca2bindingPO, title={Ca2+-binding properties of a unique ATPase inhibitor protein isolated from mitochondria of bovine heart and rat skeletal muscle.}, author={E. Yamada and Norman J. Huzel}, journal={Cell calcium}, year={1985}, volume={6 6}, pages={469-79} }