Comparative Experiments of Protein Denaturation for Studying Structural Difference of Homologous Membrane Proteins: P-450_<scc> and P-450_<11β>

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The topological difference between two homologous membrane proteins, cytochromes P-450_<scc> and P-450_<11β> in the inner membrane of bovine adrenocortical mitochondria, was studied by denaturation experiments, using urea and 1-pentanol as denaturants. Both P-450s denatured at the urea concentration of about 2.5 M that is in the concentration range of the denaturation of soluble proteins. In contrast, P-450_<11β> was denatured by 1-pentanol, which is an efficient denaturant of membrane proteins, at a much lower concentration than P-450_<scc>. These results suggested that the membrane domain is more strongly coupled with the soluble functional domain in P-450_<11β> than P-450_<scc>. It was also indicated that the comparative experiments of protein denaturation by urea and alcohol provide a simple method to identify the structural difference of homologous membrane proteins.
社団法人応用物理学会の論文
1999-01-15