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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