A coupling factor from sarcoplasmic reticulum required for the translocation of Ca2+ ions in a reconstituted Ca2+ATPase pump.
作者： E Racker , E Eytan
DOI: 10.1016/S0021-9258(19)40975-7
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摘要: 1. During purification of the Ca2+ATPase from sarcoplasmic reticulum rabbit muscle, different fractions with similar activity were found to vary greatly in their ability catalyze 45Ca2+ translocation reconstituted liposomal systems. 2. A heat-stable fraction isolated most active Ca2+ enhanced several-fold rate least fraction. It also increased ratio ATP hydrolysis over 5-fold. The properties coupling factor resemble those proteolipid previously described by MacLennan et al. (MACLENNAN, D.H., YIP, C. C., ILES, G. H., and SEAMAN, P. (1972) Cold Spring Harbor Symp. Quant. Biol. 37, 469-478). 3. When was added either fragments or liposomes after, rather than before, reconstitution, it acted as an ionophore abolishing translocation.
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