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Yim, Sung-Kun,Yun, Su-Jung,Yun, Chul-Ho Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.5
NADPH-cytochrome P450 reductase (CPR) transfers electrons from NADPH to cytochrome P450, and catalyzes the one-electron reduction of many drugs and foreign compounds. Various forms of spectrophotometric titration have been performed to investigate the electron-accepting properties of CPR, particularly, to examine its ability to reduce cytochrome c and ferricyanide. In this study, the reduction of 1,1-diphenyl-2-picrylhydrazyl (DPPH) by CPR was assessed as a means of monitoring CPR activity. The principle advantage of DPPH is that its reduction can be assayed directly in the reaction medium by a continuous spectrophotometry. Thus, electrons released from NADPH by CPR were transferred to DPPH, and DPPH reduction was then followed spectrophotometrically by measuring $A_{520}$ reduction. Optimal assay concentrations of DPPH, CPR, potassium phosphate buffer, and NADPH were first established. DPPH reduction activity was found to depend upon the strength of the buffer used, which was optimal at 100 mM potassium phosphate and pH 7.6. The extinction coefficient of DPPH was $4.09\;mM^{-1}\;cm^{-1}$. DPPH reduction followed classical Michaelis-Menten kinetics ($K_m\;=\;28\;{\mu}M$, $K_{cat}\;=\;1690\;min^{-1}$). This method uses readily available materials, and has the additional advantages of being rapid and inexpensive.
Yim Sung-Kun,Ahn Taeho,Jung Heung-Chae,Pan Jae-Gu,Yun Chul-Ho The Pharmaceutical Society of Korea 2005 Archives of Pharmacal Research Vol.28 No.4
Human cytochromes P450 (GYP) 2A6 and 2E1 are of great interest because of their important roles in the oxidation of numerous drugs and carcinogens. Bacterial expression systems, especially Escherichia coli cells, have been widely used for the production of various GYP enzymes in order to obtain high yield of proteins. The expression methods usually employ longer culture time (30-72 h) at lower temperature (usually under $30^{\circ}C$). Expression levels of GYPs 2A6 and 2E1 at $37^{\circ}C$ were compared to those at $28^{\circ}C$, which is a usual temperature used in most bacterial expression systems for human GYP expression. Within 18 h the expression levels of GYPs 2A6 and 2E1 reached up to 360 and 560 nmol per liter culture at $37^{\circ}C$, respectively, which are compatible with those of 36 h culture at $28^{\circ}C$. The activities of GYPs expressed at $37^{\circ}C$ were also comparable to those expressed at $28^{\circ}C$. The present over-expression system can be useful for rapid production of large amounts of active human GYPs 2A6 and 2E1 in E. coli.
Sung-Kun Yim,Dae-Won Ki,두홍수,Hyuk Kim,권태호 한국생물공학회 2016 Biotechnology and Bioprocess Engineering Vol.21 No.6
The biochemical properties of Spirulina platensis in an internally illuminated photobioreactor (IlPBR) were investigated under different light-emitted diode (LED) wavelengths; blue (λmax= 450 and 460 nm), green (λmax= 525 nm), red (λmax = 630 and 660 nm), and white (6,500K), with various light intensities (200, 500, 1,000, and 2,000 μmol/m2/sec) were examined. The highest specific growth rate, maximum biomass, and phycocyanin productivity occurred under the red LEDs (0.39/day, 0.10 g/L/day, and 0.14 g/g-cell/day, respectively) at 1,000 μmol/m2/sec; the lowest growth rate was obtained under blue LEDs. Indeed, the size of trichomes was changed into short form under blue LEDs at all light intensities or all LEDs at 2,000 μmol/m2/sec for the first 2 days after inoculation, and S. platensis did not grow in the IlPBR under the dark condition. These results provide a base for different approaches for designing the pilot scale photobioreactor and developing cost-effective light sources.
Yim, Sung-Kun,Yun, Chul-Ho,Ahn, Tae-Ho,Jung, Heung-Chae,Pan, Jae-Gu Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.3
NADPH-cytochrome P450 reductase (CPR) transfers electrons from NADPH to cytochrome P450 and also catalyzes the one-electron reduction of many drugs and foreign compounds. Various spectrophotometric assays have been performed to examine electron-accepting properties of CPR and its ability to reduce cytochrome $b_5$, cytochrome c, and ferricyanide. In this report, reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) by CPR has been assessed as a method for monitoring CPR activity. The principle advantage of this substance is that the reduction of MTT can be assayed directly in the reaction medium by a continuous spectrophotometric method. The electrons released from NADPH by CPR were transferred to MTT. MTT reduction activity was then assessed spectrophotometrically by measuring the increase of $A_{610}$. MTT reduction followed classical Michaelis-Menten kinetics ($K_m\;=\;20\;{\mu}M$, $k_{cat}\;=\;1,910\;min^{-1}$). This method offers the advantages of a commercially available substrate and short analysis time by a simple measurement of enzymatic activity of CPR.