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- W1549773414 abstract "Abstract A protein has been isolated from calf heart inner mitochondrial membrane with the aid of an electron paramagnetic resonance (EPR) assay based on the relative binding properties of Ca2+, Mn2+, and Mg2+ to the protein. The molecular weight of this protein has been estimated to be about 3000 by urea/sodium dodecyl sulfate-gel electrophoresis and amino acid analysis. The isolated protein has been shown to have high affinity and high specificity for Ca2+ (Jeng, A. Y., Ryan T. E., and Shamoo, A. E. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 2125-2129). However, the protein was found to be contaminated with a large amount of phospholipids. There are 150 mol of phospholipids associated with each mole of the protein. The protein is delipidated using Sephadex LH-20 column chromatography. The contaminating phospholipids can be reduced to 0.1 mol of phospholipids/mol of protein. There are no detectable free fatty acids, hexosamines, or sialic acids associated with the delipidated protein. This protein is named calciphorin, meaning calcium ionophore protein." @default.
- W1549773414 created "2016-06-24" @default.
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- W1549773414 date "1980-07-01" @default.
- W1549773414 modified "2023-10-14" @default.
- W1549773414 title "Isolation of a Ca2+ carrier from calf heart inner mitochondrial membrane." @default.
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- W1549773414 doi "https://doi.org/10.1016/s0021-9258(18)43659-9" @default.
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