TY - JOUR
AU - Stell, J G P
AB - 51P C. Stubley and J.G.P. Stell, University of Bradtord, Department of Pharmaceutical BD7 lDP, West Yorkshire. Chemistry, Bradford, The liver cytosol enzyme, aldehyde oxidase, plays an important role in the oxidation of a number of drugs. Previous work has shown that this hepatic enzyme is very active in vitro towards various unsubstituted azanaphthalenes (Stubley 1979a). The present study describes the effects of substitution on these hetero- cycles with a view to extending existing knowledge of the substrate-binding site. The rates of oxidation of the compounds were followed by monitoring spectrophoto- metrically the reduction of potassium ferricyanide which occurs subsequent to the reduction of the enzyme by substrate. Km values were determined using either crude fractions of enzyme free from cytochrome c or highly purified enzyme fractions prepared by gel chromatography. Table 1 Compounds Tested as Substrates of Aldehyde Oxidase -1 NO (-) or little (*) activity Substrate Km (mol. litre ) -3 Quinoline 3 x Pyridine - Pyrazine - 3-Me thylquinoline 5 x 1 s oquino 1 ine 1.96 x Pyrimidine * 3-Me thy lisoquino line 2.47 x lod6 Pyradazine Phenan thri dine.'. < 10 5,6-Benzoquinoline - 8-Me thy lquinol ine * 7,8-Benzoquinoline - kKm determined by following reduction 
TI - Investigation of the Substrate-Binding Site of Aldehyde Oxidase
JO - Journal of Pharmacy and Pharmacology: An International Journal of Pharmaceutical Science
DO - 10.1111/j.2042-7158.1980.tb10854.x
DA - 1980-12-01
UR - https://www.deepdyve.com/lp/oxford-university-press/investigation-of-the-substrate-binding-site-of-aldehyde-oxidase-280ODe6xHT
SP - 51P
EP - 51P
VL - 32
IS - Supplement_1
DP - DeepDyve
ER -