Cytochrome P450 1A2: Oligomers in Proteoliposomes

K. N. Myasoedova

Semenov Institute of Chemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 117977 Russia; fax: (095) 939-7417; E-mail: kinet@glas.apc.org

Received April 9, 1999

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The presence of oligomers of cytochrome P450 1A2 in membranes of proteoliposomes produced by the cholate-dialysis technique was demonstrated by cross-linking of protein molecules with bifunctional reagents followed by electrophoretic analysis of the modified proteins. A hexameric organization of cytochrome P450 1A2 in the membrane of proteoliposomes is suggested with high probability based on the comparison of the purified hemoprotein oligomeric structure in an aqueous medium and that in the proteoliposomes. The comparison was carried out using the same method.

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KEY WORDS: microsomal cytochrome P450, form 1A2, quaternary structure, proteoliposomes, bifunctional reagents

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