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Cytochrome expression

Taken together, these experiments indicate that human recombinant cytochromes expressed in E. coli are characterized by substrate specificities, reaction rates, turnover numbers and specific inhibition profiles in keeping with the counterpart enzymes from human liver microsomes. [Pg.1619]

Komori M, Nishio K, Kitada M, et al. 1990. Fetus-specific expression of a form of cytochrome P-450 in human liver. Biochemistry 29 4430-4433. [Pg.217]

Coplanar PCBs, PCDDs, and PCDFs express Ah-receptor-mediated toxicity (Chapter 6, Section 6.2.4). Binding to the receptor leads to induction of cytochrome P4501 and a number of associated toxic effects. Again, toxic effects are related to the extent of binding to this receptor and appear to be additive, even with complex mixtures of planar polychlorinated compounds. Induction of P4501A1/2 has been widely used as the basis of a biomarker assay. Residue data can be used to estimate TEQs for dioxin (see Chapter 7, Section 7.2.4). [Pg.246]

Majdic, G., Sharpe, R.M., and Oshaughnessy, PJ. et al. (1996). Expression of cytochrome P450 17 alpha-hydroxylase/C 17-20 lyase in the fetal rat testis is reduced by maternal exposure to exogenous estrogens. Endocrinology 137, 1063-1070. [Pg.359]

Shao ZQ, R Behki (1996) Characterization of the expression of the thcB gene, coding for a pesticide-degrading cytochrome P450 in Rhodococcus strains. Appl Environ Microbiol 62 403-407. [Pg.334]

Figure 2 shows the effect of flow rate on column efficiency using the SW-2000 column with cytochrome C. The column efficiency expressed as the number of theoretical plates (N) was dependent on flow rate, a result typical of size exclusion chromatography. [Pg.288]

Jaffe, H.A., Buhl, R., Borok, Z., Trapnell, B. and Crystal, R.G. (1989). Activated alveolar macrophages express increased levels of cytochrome b245 heavy chain mRNA transcripts correlating with enhanced capacity to release oxidants. Clin. Res. 37, 477A. [Pg.229]

Figure 3.9 MALDITOF mass spectrum showing over-expressed soluble core domain protein of cytochrome B5. Figure 3.9 MALDITOF mass spectrum showing over-expressed soluble core domain protein of cytochrome B5.
Goodacre, R. Karim, A. Kaderbhai, M. A. Kell, D. B. Rapid and quantitative analysis of recombinant protein expression using pyrolysis mass spectrometry and artificial neural networks Application to mammalian cytochrome b5 in Escherichia coli. J. Biotechnol. 1994,34,185-193. [Pg.124]


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See also in sourсe #XX -- [ Pg.78 ]

See also in sourсe #XX -- [ Pg.363 ]




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