Electrophoretic behavior of the H+-ATPase proteolipid from bovine heart mitochondria |
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Authors: | Jan Kopecký Josef Hou?těk Eva Szarska Zdeněk Drahota |
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Institution: | (1) Institute of Physiology, Czechoslovak Academy of Sciences, Vídeská 1083, CS-142 20 Prague 4, Czechoslovakia |
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Abstract: | The proteolipid subunit of H+-ATPase was labeled by 14C]N,N-dicyclohexylcarbodiimide in bovine heart mitochondria. The radioactive labeling was followed using various systems of sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). When using discontinuous SDS-PAGE (Laemmli, U.K., 1970,Nature (London)227, 680–685) a monomeric (Mr 7600±1500) and a dimeric form (Mr 17,800±1200) of the proteolipid were detected, while only the monomeric form was found on urea (8 M) containing gels (SDS-PAGE according to Laemmli; or Swank, R. T., and Munkers, K. D., 1971,Anal. Biochem.
39, 462–477). When using SDS-PAGE with Na-Pi buffer (Weber, K., and Osborn, M., 1969,J. Biol. Chem.
244, 4406–4442), only a dimeric form of the proteolipid (Mr 15,000±1000) was detected. Experimental data indicate that the different patterns of proteolipid separation are related to the presence of the two distinct proteolipid conformations in the SDS solution. |
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Keywords: | Mitochondrial H+-ATPase bovine heart proteolipid conformations gel electrophoresis dicyclohexylcarbodiimide |
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