Abstract
Proteoliposomes, containing cytochrome P450 1A2, were obtained by the cholate-dialysis technique. The effect of bifunctional cross-linking reagents on the purified hexameric cytochrome P450 1A2 in an aqueous medium and on the proteoliposomal P450 1A2 have been compared. Electrophoretic analysis of the modified proteins demonstrated the same oligomeric (hexameric) organization of the hemoprotein in each case.
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REFERENCES
Robinson, N. S. and Talbert, L. (1986) Triton X-100 induced dissociation jf beef heart cytochrome c oxidase into monomers. Biochemistry 25:2328-2335.
Tsuprun, V. L. et al. (1985) Hexameric organization of cytochrome P-450 from liver microsomes. Dokl. Acad. Nauk SSSR 285:1496-1499.
Tsuprun, V. L. et al. (1986) Quaternary structure of the liver microsomal cytochrome P-450. FEBS Lett. 205:35-40.
Myasoedova, K. N. (1993) Hexameric organization of cytochrome P-450 LM4 from rabbit hepatocyte endoplasmic reticulum membranes. Biochemistry (Moscow) 58:894-898.
Myasoedova, K. N. and Tsuprun, V. L. (1993) Cytochrome P-448: studies on the oligomeric structure. Dokl. RAN 328:403-406.
Myasoedova K. N. and Tsuprun, V. L. (1993) Cytochrome P-450; hexameric structure of the purfied LM4 form. FEBS Lett. 325: 251-254.
Myasoedova, K. N. and Berndt, P. (1990) Structural organization of cytochrome P-450 oligomers: a study on immobilized form LM2, Biokhimiya 55:155-164.
Myasoedova, K. N. and Berndt, P. (1990) Immobilized cytochrome P-450 LM2. Dissociation and reassociation of oligomers. FEBS Lett. 270:177-180.
Myasoedova, K. N. (1998) Specificity of self-assembly of cytochrome P450 oligomers. Biochemistry (Moscow) 63:1395-1399.
Myasoedova, K. N. and Berndt, P. (1989) A method for cytochrome P-450 LM2 immobilization with retaining of its catalytic activity. Biol. Nauki 4:18-25.
Davidov, D. R., Karyakin, A. V., Binas, B., Kurganov, B. I., and Archakov, A. I. (1985) Kinetic studies on cytochrome P-450 reduction by dithionite. Europ. J. Biochem 150:155-159.
Johnson, E. F., Schwab, G. E., and Vickery, L. E. (1988) Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c J. Biol. Chem. 263:17672-17677.
Myasoedova, K. N. and Berndt, P. (1989) Cytochrome P-450 in proteoliposomes: the oligomeric structure of isoform LM2. Biokhimiya 54:1445-1456.
Myasoedova, K. N. and Berndt, P. (1990) Cytochrome P-450 LM2 oligomers in proteoliposomes. FEBS Lett. 275:235-238.
Imai, Y., Hashimoto-Yutsudo, C., Satake, H., Girardin, A., and Sato, R. (1980) Multiple forms of cytochrome P-450 purified from liver microsomes of phenobarbital-and 3-methylcholanthrene-pretreated rabbits. 1. Resolution, purification, and molecular properties. J. Biochem. 88:489-504.
Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. J. Biol. Chem. 239:2370-2385.
Hashimoto-Yutsudo, C., Imai, Y., and Sato, R. (1980) Multiple forms of cytochrome P-450 purified from liver microsomes of phenobarbital-and 3-methylcholanthrene-pretreated rabbits. II. Spectral properties. J. Biochem. 88:505-516.
Asryants, R. A., Duszenkova, I. V., and Nagradova, N. K. (1985) Determination of sepharose-bound protein with coomassie brilliant blue G-250. Analyt. Biochem. 151:571-574.
Bosterling, B. and Trudell, J. R. (1982) Association of cytochrome b 5 and cytochrome P-450-reductase with cytochrome P-450 in the membrane of reconstituted vesicles. J. Biol. Chem. 257:4783-4787.
Ekstrom, G. and Ingelman-Sundberg, M. (1986) Mechanisms of lipid peroxidation dependent upon cytochrome P-450 LM2. Europ. J. Biochem. 158:195-201.
Ingelman-Sundberg, M., Blank, J., Smettan, G., and Ruckpaul, K. (1983) Reduction of cytochrome P-450 LM2 by NADPH in reconstituted phospholipid vesicles in dependent on membrane charge. Europ. J. Biochem. 134:157-162.
Kominami, S., Itho, Y., and Takemory, S. (1986) Studies on the interaction of steroid substrates with adrenal microsomal cytochrome P-450 (P-450 c21) in liposome membranes. J. Biol. Chem. 261:2077-2083.
Nishimoto, Y., Kinosita, K. J., and Ikegami, A. (1983) Possible association of NADPH-cytochrome P-450 reductase and cytochrome P-450 in reconstituted phospholipid vesicles. Biochemistry 22:3586-3594.
Davis, G. E. and Stark, G. R. (1970) Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of ligomeric protein. Proc. Natl. Acad. Sci. U.S.A. 66:651-656.
Friederich, P. (1986) Enzymes. A Quaternary Structure and Supermolecular Complexes [Russian translation], Mir, Moscow.
Nelson, D. R. and Strobel, H. W. (1988) On the membrane topology of vertebrate cytochrome P-450 proteins. J. Biol. Chem. 263:6038-6050.
Berndt, P., Magretova, N. N., Myasoedova, K. N., and Chernyak, V. Ya. (1989) Cytochrome P-450 LM2 hexamer dissociation in the presence of nonionic detergent emulgen 913. Biokhimiya 54:338-341.
Wachenfeldt, C., Richardson, T. H., Cosme, J., and Johnson, E. F. (1997) Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modifications of its N-terminus. Arch. Biochem. Biophys. 339:107-114.
Greinert, R., Finch, S. A. E., and Stier, A. (1982) Conformation and rotational diffusion of cytochrome P-450 changed by substrate binding. Biosci. Rep. 2:991-994.
Schwarz, D., Pirrwitz, J., Coon, M. J., and Ruckpaul, K. (1982) Mobility and clusterlike organization of liposomal cytochrome P-450 LM2. Saturation transfer EPR-studies. Acta biol. med. germ. 41:425-430.
Kim, I. C. (1982) Immunological characterization of cytochrome H-450 in rat tissue. J. Biol. Chem. 257:1063-1070.
Tsuprun, V. L. et al. (1987) Electron microscopy of methanemonooxygenase from methane oxidizing bacteria Methylococcus capsulatus. Dokl. Acad. Nauk SSSR 292:490-494.
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Myasoedova, K.N., Magretova, N.N. Cross-Linking Study of Cytochrome P450 1A2 in Proteoliposomes. Biosci Rep 21, 63–72 (2001). https://doi.org/10.1023/A:1010486118448
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DOI: https://doi.org/10.1023/A:1010486118448