European journal of biochemistry, 225(3), 959-965 (1994-11-01)
Interactions of two distinct quinoprotein amine oxidases from Aspergillus niger, AO-I and AO-II, with active-site covalent modifiers have been investigated. Both enzymes are inhibited similarly by phenylhydrazine or p-nitrophenylhydrazine, forming an orange Schiff base with a carbonyl group of topaquinone
Pig kidney diamine oxidase was purified to homogeneity. The reaction product of the cofactor with p-nitrophenylhydrazine (pNPH) was liberated with pronase treatment and purified. 1H NMR, uv/vis, and electrospray tandem mass spectroscopy revealed it to be a dipeptide with the
Journal of the American Chemical Society, 125(20), 6113-6125 (2003-06-06)
4-n-Butylamino-5-ethyl-1,2-benzoquinone (1(ox)) has been synthesized as a model compound for the LTQ (lysine tyrosyl quinone) cofactor of lysyl oxidase (LOX). At pH 7, 1(ox) has a lambda(max) at 504 nm and exists as a neutral o-quinone in contrast to a
Comparative biochemistry and physiology. B, Comparative biochemistry, 86(1), 135-139 (1987-01-01)
The total plasmalogen content of lingual and other tissues was analyzed using the iodine-addition (Method 1), the p-nitrophenylhydrazone (Method 2), and the two-dimensional thin layer chromatography procedure (Method 3). Methods 1 and 2 were simple, rapid and reproducible, yielding values
Journal of inorganic biochemistry, 56(2), 127-141 (1994-11-01)
An improved purification scheme for an amine oxidase from equine plasma (EPAO), a nonruminant source, is described and the protein's active-site is characterized. EPAO is dimeric and contains one Type-2 Cu(II) ion per monomer. The EPAO Cu(II) site is spectroscopically