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
Biochimica et biophysica acta, 1295(1), 59-72 (1996-06-07)
Amine oxidases (EC 1.4.3.6) from Aspergillus niger, AO-I (2 x 75 kDa) and AO-II (80 kDa), were examined to determine the cofactor structure. Inactivated with p-nitrophenylhydrazine, they showed absorption and fluorescence spectra similar to those published for other copper amine
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
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