Search

Your search keyword '"Azari, Mahmood"' showing total 30 results
Start Over Author "Azari, Mahmood"
30 results on '"Azari, Mahmood"'

9. A study of cytochrome P-448, a component of the monooxygenase system from Saccharomyces ceresvisiae : purification and characterization

Author

Azari, Mahmood Rezazadeh

Subjects
572, Biochemistry
Abstract

The effect of glucose concentration in growth medium on biosynthesis of cytochrome P-450/P-448 under aerobic and anaerobic conditions was examined. High glucose concentration was required in both cases. The cytochrome P-450 enzyme from yeast Saccharomyces cerevisiae showed a Soret peak in the reduced CO-difference spectrum at 448nm, was purified to homogenity and had a molecular weight of 55,500. Cytochromes c(P-450) reductase, b[5], b[5] reductase were also purified from the same microsomal preparation. Amino acid analysis of yeast cytochrome P-448 revealed the presence of 407 residues per molecule. The sum of molecular weight of the polypeptides and other components was in good agreement with the molecular weight value obtained from SDS-polyacrylamide gel electrophoresis. A reconstituted system of purified yeast cytochrome P-448, NADPH:cytochrome c(P-450) reductase and phospholipid showed benzo(a)pyrene hydroxylase activity. The spin state of substrate-free and benzo(a)pyrene-bound purified yeast cytochrome P-448 were 94% and 82% low spin at 22°C respectively. Equilibrium gel filtration analysis of the number of benzo(a)pyrene binding sites per mole of enzyme monomer showed a value of 1 for purified yeast cytochrome P-448 and 6 for this enzyme in microsomal form. In addition to benzo(a)pyrene, lanosterol, ethylmorphine, dimethylnitrosamine and sodium phenobarbitone showed Type I binding spectra with yeast cytochrome P-448. A more specific and efficient form of benzo(a)pyrene hydroxylase was induced by the addition of benzo(a)pyrene to the yeast growth medium at zero time. Based on the effect of modification of various amino acids on parameters of yeast cytochrome P-448, participation of -SH group(s) and tyrosyl residue(s) in the active site of this enzyme is suggested. Various supports were evaluated for immobilization of yeast cytochrome P-448. Calcium alginate was found to be especially useful. Cytochrome P-448 from Saccharomyces cerevisiae is identified as a distinct enzyme of the cytochrome P-450 family. This enzyme, however, has many properties in common with cytochrome P-448 from mammalian sources.

Published
1984

10. Impacts of future land cover and climate change on the water balance in northern Iran

Author

Shayesteh, Kamran [0000-0002-8451-058X], Serrano Notivoli, Roberto [0000-0001-7663-1202], López-Moreno, Juan Ignacio [0000-0002-7270-9313], Shooshtari, Sharif Joorabian, Shayesteh, Kamran, Gholamalifard, Mehdi, Azari, Mahmood, Serrano-Notivoli, Roberto, López-Moreno, Juan I., Shayesteh, Kamran [0000-0002-8451-058X], Serrano Notivoli, Roberto [0000-0001-7663-1202], López-Moreno, Juan Ignacio [0000-0002-7270-9313], Shooshtari, Sharif Joorabian, Shayesteh, Kamran, Gholamalifard, Mehdi, Azari, Mahmood, Serrano-Notivoli, Roberto, and López-Moreno, Juan I.

Abstract

We evaluated the potential impacts of future land cover change and climate variability on hydrological processes in the Neka River basin, northern Iran. This catchment is the main source of water for the intensively cultivated area of Neka County. Hydrological simulations were conducted using the Soil and Water Assessment Tool. An ensemble of 17 CMIP5 climate models was applied to assess changes in temperature and precipitation under the moderate and high emissions scenarios. To generate the business-as-usual scenario map for year 2050 we used the Land Change Modeler. With a combined change in land cover and climate, discharge is expected to decline in all seasons except the end of autumn and winter, based on the inter-model average and various climate models, which illustrated a high degree of uncertainty in discharge projections. Land cover change had a minor influence on discharge relative to that resulting from climate change.

Published
2017

16. Climate change impacts on streamflow and sediment yield in the North of Iran.

Author

Azari, Mahmood, Moradi, Hamid Reza, Saghafian, Bahram, and Faramarzi, Monireh

Subjects
*STREAMFLOW, *CLIMATE change, *RIVER sediments, *HYDROLOGIC cycle, *RIVERS
Abstract

Climate change will accelerate the hydrological cycle, altering rainfall, and the magnitude and timing of runoff. The purpose of this paper is to assess the impacts of climate change on streamflow and sediment yield from the Gorganroud river basin in the North of Iran. To study the effects of climatic variations, the SWAT model was implemented to simulate the hydrological regime and the SUFI-2 algorithm was used for parameter optimization. The climate change scenarios were constructed using the outcomes of three general circulation models for three emission scenarios. The study results for 2040–2069 showed an increase in annual streamflow of 5.8%, 2.8% and 9.5% and an increase in sediment yield of 47.7%, 44.5% and 35.9% for the A1F1, A2 and B1 emission scenarios, respectively. This implies that the impact of climate change on sediment yield is greater than on streamflow. Monthly variations show that the increase in discharge and sediment yield is more pronounced in wet seasons and the decrease is more pronounced in summer (July–September). The results highlighted the strong impact of climate change and reflected the importance of incorporating such analysis into adaptive management.Editor Z.W. Kundzewicz Associate editor Not assigned [ABSTRACT FROM AUTHOR]

Published
2016
Full Text
View/download PDF

17. Evaluation and Validation of Virus Removal by Ultrafiltration During the Production of Diaspirin Crosslinked Haemoglobin (DCLHb)

Author

Azari, Mahmood, primary, Boose, Jeri Ann, additional, Burhop, Kenneth E., additional, Camacho, Theresa, additional, Catarello, James, additional, Darling, Alan, additional, Ebeling, August A., additional, Estep, Timothy N., additional, Pearson, Luisa, additional, Guzder, Sarosh, additional, Herren, Janelle, additional, Ogle, Kristen, additional, Paine, Jennifer, additional, Rohn, Kimberly, additional, Sarajari, Ramin, additional, Sun, Chong-Son, additional, and Zhang, Liang, additional

Published
2000
Full Text
View/download PDF

18. Simulation of a New Forward Converter Using SDSR Technology with High Efficiency.

Author

Azari, Mahmood, Delshad, Majid, and Borzabadi, Ebrahim

Subjects
CASCADE converters, ELECTRIC current converters, ELECTRIC potential, ELECTRIC circuits, ELECTRIC lines, TRANSISTORS, ELECTRONICS
Abstract

In this study, a new forward converter with self driven synchronous rectification (SDSR) with high efficiency and low output voltage has been introduced. In the proposed converter, soft switching conditions (ZCS turn on and ZVS turn off) for main switch, via an auxiliary circuit is provided. However, auxiliary circuit does not use any extra switch and as a result, extra driver is not needed. Since the number of turns of auxiliary transformer is very low , so does not impose high conductive loss of the proposed converter and in output circuit the two side transistors switch with very low conductive loss are used and also soft switching condition are prepared for them. The converter is controlled by PWM (pulse width modulation) and as a result, implementing its control circuit is very simple. To confirm theoretical analysis, the introduced converter has been simulated by Pspice. [ABSTRACT FROM AUTHOR]

Published
2012

19. A study of cytochrome P-448, a component of the monooxygenase system from Saccharomyces ceresvisiae: Purification and characterization

Author

Azari, Mahmood Rezazadeh.

Abstract

The effect of glucose concentration in growth medium on biosynthesis of cytochrome P-450/P-448 under aerobic and anaerobic conditions was examined. High glucose concentration was required in both cases. The cytochrome P-450 enzyme from yeast Saccharomyces cerevisiae showed a Soret peak in the reduced CO-difference spectrum at 448nm, was purified to homogenity and had a molecular weight of 55,500. Cytochromes c(P-450) reductase, b[5], b[5] reductase were also purified from the same microsomal preparation. Amino acid analysis of yeast cytochrome P-448 revealed the presence of 407 residues per molecule. The sum of molecular weight of the polypeptides and other components was in good agreement with the molecular weight value obtained from SDS-polyacrylamide gel electrophoresis. A reconstituted system of purified yeast cytochrome P-448, NADPH:cytochrome c(P-450) reductase and phospholipid showed benzo(a)pyrene hydroxylase activity. The spin state of substrate-free and benzo(a)pyrene-bound purified yeast cytochrome P-448 were 94% and 82% low spin at 22°C respectively. Equilibrium gel filtration analysis of the number of benzo(a)pyrene binding sites per mole of enzyme monomer showed a value of 1 for purified yeast cytochrome P-448 and 6 for this enzyme in microsomal form. In addition to benzo(a)pyrene, lanosterol, ethylmorphine, dimethylnitrosamine and sodium phenobarbitone showed Type I binding spectra with yeast cytochrome P-448. A more specific and efficient form of benzo(a)pyrene hydroxylase was induced by the addition of benzo(a)pyrene to the yeast growth medium at zero time. Based on the effect of modification of various amino acids on parameters of yeast cytochrome P-448, participation of -SH group(s) and tyrosyl residue(s) in the active site of this enzyme is suggested. Various supports were evaluated for immobilization of yeast cytochrome P-448. Calcium alginate was found to be especially useful. Cytochrome P-448 from Saccharomyces cerevisiae is identified as a distinct enzyme of the cytochrome P-450 family. This enzyme, however, has many properties in common with cytochrome P-448 from mammalian sources.

Published
1984

Catalog

Books, media, physical & digital resources
See catalog results