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  1. Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry
  2. Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 2
  3. Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 2, Issue 1, March 2008
  4. Identification of human liver cytochromes P450 by using MALDI-TOF mass spectrometry
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Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 11
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 10
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 9
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 8
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 7
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 6
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 5
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 4
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 3
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 2
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 2, Issue 4, December 2008
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 2, Issue 3, September 2008
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 2, Issue 2, June 2008
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 2, Issue 1, March 2008
Biological activity of phytosterols and their derivatives
Nitric oxide. Potentiation of NO-dependent activation of soluble guanylate cyclase: (Patho)physiological and pharmacotherapeutic importance
The methods of quantitative proteomics
Identification of human liver cytochromes P450 by using MALDI-TOF mass spectrometry
Computer-aided design of polyketides with the required properties
The role of PAR1 in protective action of activated protein C during nonimmune activation of mast cells
Antirheumatic activity of methotrexate in phospholipid nanoparticles (Phosphogliv)
Substituted aminophenols and flavonoids as potential components for test-systems for total antioxidant activity
Biodegradation of $^{125}$I-Labeled monoclonal antibodies after intravenous administration to rats with experimental C6 glioma
Polyelectrolyte microcapsules as the systems for delivery of biologically active substances
Study of the binding of nuclear proteins from Plasmodium berghei strains with different chloroquine sensitivity to oligonucleotides corresponding to regulatory elements of the multidrug resistance gene
Ubiquitin causes selective increase in the sensitivity of rat brain mitochondrial monoamine oxidases to various proteases
Distribution of mutations of acid β-D-glucosidase Gene (GBA) among 68 Russian patients with Gaucher’s disease
Functional activity of phagocytes of bronchoalveolar lavage in patients with fibro-cavernous and infiltrative pulmonary tuberculosis
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry : Volume 1

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Identification of human liver cytochromes P450 by using MALDI-TOF mass spectrometry

Content Provider Springer Nature Link
Author Petushkova, N. A. Lisitsa, A. V. Karuzina, I. I. Zgoda, V. G. Sheremetyeva, G. F. Samenkova, N. F. Nikitin, I. P. Sakharova, T. A. Kopylov, A. T. Archakov, A. I.
Copyright Year 2008
Abstract Proteomic approaches have been used for detection and identification of cytochromes P450 forms from highly purified membrane preparations of human liver. These included the protein separation by 2D-and/or 1D-electrophoresis and molecular scanning of a SDS-PAGE gel fragment in a range 45–66 kDa (this area corresponds molecular weights of cytochromes P450). The analysis of protein content was statistically evaluated by means of an original 1D-ZOOMER software package which allowed to carry out the processing of mass spectra mixture instead of individual mass spectra used by standard techniques. In the range 45–66 kDa we identified 13 microsomal membrane proteins including such cytochrome P450 forms as CYPs 1A2, 1B1, 2A6, 2E1, 2C8, 2C9, 2C10, 2D6, 3A4, 4A11, 4F2. Study of enzymatic activities of human liver microsomal cytochrome P450 isoforms CYP 1A, 2B, 3A, and 2E revealed the decrease in the rates of O-dealkylation and N-demethylation catalyzed by CYP 450 1A1/1A2 and 3A4 under pathological conditions, whereas 7-benzyloxyresorufin-O-debenzylase activity (which characterizes the total activity of CYP 2B and CYP 2C), the activities of CYP 2E1 (methanol oxidation), 7-pentoxyresorufin-O-dealkylation (CYP 2B), 7-ethoxy-and 7-methoxycoumarin-O-dealkylases (CYP 2B1) remained basically unchanged.
Starting Page 47
Ending Page 54
Page Count 8
File Format PDF
ISSN 19907508
Journal Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry
Volume Number 2
Issue Number 1
e-ISSN 19907516
Language English
Publisher Nauka/Interperiodica
Publisher Date 2008-04-03
Publisher Place Moscow
Access Restriction One Nation One Subscription (ONOS)
Subject Keyword microsomes liver cytochromes P450 microsomal oxidation one dimensional (1D) and two dimensional (2D) electrophoresis mass spectrometry Bioorganic Chemistry Medicinal Chemistry
Content Type Text
Resource Type Article
Subject Biochemistry Clinical Biochemistry Molecular Medicine
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