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 biochemistry, 123(2), 240-246 (1998-04-16)
Compositional analyses of heparin (Hep) and heparan sulfate (HS) have been undertaken with disaccharide units obtained by either enzymatic digestion with heparitinases or hydrazinolysis/deamination reaction of polysaccharides. Unsaturated disaccharide units generated by the enzymatic method are detectable on HPLC with
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
Journal of AOAC International, 77(3), 748-751 (1994-05-01)
Three spectrophotometric methods were developed for the microdetermination of decamethrin in insecticidal formulations and in water. The methods are based on the hydrolysis of decamethrin with methanolic KOH to 3-phenoxybenzaldehyde; condensation of the hydrolysis product with 2,4-dinitrophenylhydrazine (2,4-DNPH), 4-nitrophenyl-hydrazine (4-NPH)
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
