6527-33-9Relevant articles and documents
A process for preparing a broad pH fluorescent probe of the organic compound and use thereof (by machine translation)
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, (2018/04/03)
The present invention discloses a process for the preparation of a wide range of fluorescent probe in the pH of the organic compound, the organic compound can be produced according to the actual need to carry out any proportion of combination, and can be fixed in the hydrophilic high polymer further preparing and detecting water environment acidity and alkalinity of the product. The product can be realized to the pH value of the continuous measuring, thereby greatly improving the efficiency, sensitivity and repeatability. (by machine translation)
3,5-disubstituted-4-hydroxyphenyls linked to 3-hydroxy-2-methyl-4(1h)- pyridinone: Potent inhibitors of lipid peroxidation and cell toxicity
Bebbington, David,Monck, Nathaniel J. T.,Gaur, Suneel,Palmer, Alan M.,Benwell, Karen,Harvey, Victoria,Malcolm, Craig S.,Porter, Richard H. P.
, p. 2779 - 2782 (2007/10/03)
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Catechol O methyltransferase. VI. Affinity labeling with N haloacetyl 3,5 dimethoxy 4 hydroxyphenylalkylamines
Borchardt,Thakker
, p. 152 - 158 (2007/10/06)
Several N acyl 4 hydroxy 3,5 dimethoxy phenylalkylamines were synthesized and evaluated for ability to inactivate catechol O methyltransferase (COMT). 4 Hydroxy N iodoacetyl 3,5 dimethoxy phenylethylamine was found to rapidly and irreversibly inactivate this enzyme. The corresponding n concentrations bromoacetyl derivative also produced inactivation of COMT but at a slower rate than the N iodoacetyl derivative. The N acetyl and N fumaryl derivatives were completely inactive. Inactivation of COMT by these reagents appears to proceed by a unimolecular reaction within a dissociable complex rather than by a nonspecific bimolecular reaction. The proximity of the amino acid residue being modified relative to the site which binds the aromatic portion of these inhibitors was determined using N iodoactylphenylalkylamines of varying chain length. The number of methylene carbons separating the aromatic ring and the iodoacetamide moiety in these inhibitors did not greatly influence the binding to COMT nor did it affect how rapidly the enzyme was inactivated. From these observations it is concluded that the amino acid moiety being modified by this class of affinity labeling reagents must be relatively close to or part of the site which binds the aromatic region of these inhibitors.