Study of the mouse liver microsomes by the methods of proteome analysis

Biomeditsinskaya Khimiya

Volumn 50, Issue 4, 2004, Pages 367-375

  Kanaeva, I P ^a   Petushkova, N A ^a   Lokhov, P G ^a   Zgoda, V G ^a   Karuzina, I I ^a   Lisitsa, A V ^a   Archakov, A I ^a  

^a INSTITUTE OF BIOMEDICAL CHEMISTRY   (Russian Federation)

Author keywords

1D and 2D electrophoresis; Cytochrome P450s; Liver; Mass spectrometry; Microsomes; O dealkylation

Indexed keywords

CYTOCHROME P450; PHENOBARBITAL; PROTEOME;

ARTICLE; BIOINFORMATICS; ELECTROPHORESIS; ENZYME ACTIVITY; HUMAN; LIVER MICROSOME; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MEMBRANE; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PROTEIN SYNTHESIS; PROTEOMICS; PURIFICATION; ALKYLATION; ANIMAL; ENZYMOLOGY; MASS SPECTROMETRY; METABOLISM; POLYACRYLAMIDE GEL ELECTROPHORESIS;

ANIMALIA;

ALKYLATION; ANIMALS; CYTOCHROME P-450 ENZYME SYSTEM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MICE; MICROSOMES, LIVER; PROTEOME; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 6444232881     PISSN: 23106905     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (23)

1. Archakov A.I., Bachmanova G.I. (1990) Cytochrome P450 and Active Oxygen, Taylor and Francis, London.
2. Rozman D., Waterman M.R. (1998) Drug Metab. Dispos., 26, 1199-1201.
3. Whitlocock J.P.J., Denison M.S. (1995) in: Cytochrome P450: Structure, Mechanism, Biochemistry (Ortiz de Montellano P.R. ed.) Plenum Press: New York, p. 391.
4. Lewis D.F.V. (2001) Guide to Cytochromes P450. Structure and Function, Taylor and Francis, London and New York.
5. Galeva N., Alterman M. (2002) Proteomics, 2, 713-722.
6. Vlasuk G.P., Walz F.G.J. (1980) Anal. Biochem., 105, 112-120.
7. Vlasuk G.P., Walz F.G.J. (1982) Arch.Biochem.Biophys., 214, 248-259.
8. Omura T., Sato R. (1964) J. Biol. Chem., 239, 2379-2385.
9. Pearce R.E., McIntyre C.J., Madan A., Sanzgiri U., Draper A.J., Bullock P.L., Cook D.C., Burton A., Latham J., Nevins C., Parkinson A. (1996) Arch. Biochem. Biophys., 331, 145-169.
10. French J.S., Coon M.G. (1979) Arch. Biochem.Biophys., 195, 565-577.
11. Lowry O.H., Rosebrough N.I., Farr A.L., Randall R.J. (1951) J.Biol.Chem., 193, 265-275.
12. Burke M.D., Mayer R.T. (1983) Chem.-Biol. Interactions, 45, 243-258.
13. Laemmli U.K. (1970) Nature, 227, 680-685.
14. Neuhoff V., Arold N., Taube D., Ehrhardt W. (1988) Electrophoresis, 9, 255-262.
15. Shevchenko A., Wilm M., Vorm O., Mann M. (1996) Anal.Chem., 68, 850-858.
16. Perkins, D. N., Pappin, D. D. J., Creasy, D. M., Cottrell, J. M. (1999) Electrophoresis, 20, 3551-3567.
17. Lokhov P.G., Tikhonova O.V., Moshkovskii S.A., Goufman E.I., Serebrikova M.V., Maksimov B.I., Toropyguine I.Yu., Zgoda V.G., Govorun V.M., Archakov A.I. (2004) Proteomics (in press).
18. Pike M.G, Martin Y.N., Mays D.C., Benson L.M., Naylor S., Lipsky J.J. (1999) Alcohol Clin. Exp. Res., 23, 1173-1179.
19. Kimonen T., Juvonen R.O., Alhava E., Pasanen M. (1995) Br.J.Pharmacol., 114,832-836.
20. Blackstock W.P., Wier M.P. (1999) Trends Biotech., 17, 121-126.
21. Page M.J., Amess B., Rohlff Ch., Stubberfield C., Parekh R. (1999) Drug Discovery Today, 4, 55-62.