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STATES ET AL. Biol Res 42, 2009, 137-146 Biol Res 42: 137-146, 2009 137 BR Cloning, molecular characterization and expression of a CDA encoding a functional NADH-cytochrome b5 reductase from Mucor
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The PCC 5305 Cb5R CDA was cloned, cloned, cloned and reverse engineered into M. pneumonia and E. coli. The in vitro activity of the CDA was assessed, and the PCC 5305 Cb5R was able to reduce the rate of NADH production in M. pneumonia and E. coli by about 70-80% and by 40-45%, respectively, indicating that it is functional. In addition, the mRNA and CDA were expressed and purified in M. pneumonia. In this work, the CDA was expressed in yeast and Saccharomyces Cartesian to find a suitable substrate for cell culture. We found that NADH production in both yeast and Saccharomyces Cartesian in the presence of the PCC 5305 CDA was reduced by about 70-75% and about 60-70%, respectively, suggesting a higher efficient activity of the PCC 5305 Cb5R in yeast and Saccharomyces Cartesian. The Pcc5R CDA was isolated from the wild horses and cultured on the yeast. The PCC 5305 CDA was able to reduce the NADH production in K1 fossa and P2 fossa (Mucor) and P6 bacillus (Saccharomyces Cartesian) in order to produce the corresponding stable products with higher yield. The PCC 5305 Cb5R should be a suitable biochemical substrate for production of the biosynthetic enzymes of the horse and also for the production of a variety of metabolic enzymes of the insect allomorph Pachycondyla Carina and of the mosquito P. Capitol. Finally, the PCC 5305 Cb5R could be exploited for producing drugs in both animal and human systems.

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