Purification and properties of adenosine triphosphatase solubilized from beef heart mitochondria by chloroform |
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| Authors: | Kopecký Jan Houštěk Josef Drahota Zdeněk |
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| Affiliation: | (1) Institute of Medical Chemistry, Faculty of Medicine, Charles University, 120 00 Prague;(2) Institute of Physiology, Czechoslovak Academy of Sciences, 142 20 Prague, Czechoslovakia |
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| Abstract: | Summary Soluble, oligomycin-insensitive ATPase released from beef heart mitochondria by chloroform extraction can be further purified by Sepharose 6B gel filtration. This purification increases enzyme activity 4–5 times (100–130 U/mg). According to specific activity, high purity and ability to reconstitute oligomycin-sensitive complex, isolated ATPase is quite comparable with enzyme preparations isolated by other methods. |
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