Title : NADPH as a co-substrate for studies of the chlorinating activity of myeloperoxidase.

Pub. Date : 1999 Nov 1

PMID : 10527939






2 Functional Relationships(s)
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1 The oxidation of NADPH was characterized by a decrease in the A(339) of the reduced nicotinamide with the concomitant appearance of a new chromophore with absorbance maximum at 274 nm, characterized by isosbestic points at 300 and 238 nm. Niacinamide 2,4-dienoyl-CoA reductase 1 Homo sapiens
2 A quantitative comparison of difference spectra obtained with NADPH and NMNH indicated that chlorination occurred on the nicotinamide part of the molecule. Niacinamide 2,4-dienoyl-CoA reductase 1 Homo sapiens