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Article: New enzyme research study findings recently were published by researchers at Kumamoto University.
- Article from:
- Medical Devices & Surgical Technology Week
- Article date:
- November 15, 2009
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"The interactions of acyl-CoA with medium-chain acyl-CoA dehydrogenases (MCADs) reconstituted with artificial FADs-i.e. 8-CN-, 7,8-Cl2-, 8-Cl-, 8-OCH3- and 8-NH2-FAD-were investigated by UV-visible absorption and FT-IR measurements. Although 8-NH2-FAD-MCAD did not oxidize acyl-CoA the wavelength of the absorption maximum of the flavin was altered by acyl-CoAs binding," researchers in Kumamoto, Japan report (see also Enzyme Research).
"Thus, 8-NH2-FAD-MCAD is one of the attractive materials for investigation of enzyme-substrate (ES) interaction in ES complex (the complex of oxidized MCAD with acyl-CoA). FT-IR difference spectra between non-labelled and ...
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Article: Researchers from Kumamoto University report recent ...
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May 13, 2009 ;
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... ... and colleagues, Kumamoto University. The researchers ... contact T. Akaike, Kumamoto University, Graduate School ... Nucleotide Research, Enzyme Research, Immunology ... Salmonellosis, Synthase, Kumamoto University. This article ...
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