Purification and some properties of hamster liver aldehyde oxidase.
Aldehyde oxidase was purified from hamster liver cytosol by ammonium sulfate fractionation, chromatography on DEAE-cellulose and Phenyl-Toyopearl, and HPLC-gel filtration on TSK-gel G3000SW(XL) column. The purified enzyme was homogeneous by the criterion of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Its molecular weight was determined to be 144800 by SDS-PAGE and 288000 by HPLC gel filtration. The isoelectric point was pH 5.1. The apparent Km and Vmax for benzaldehyde and 2-hydroxypyrimidine were 19.0 and 4.4 microM, and 165 and 211 nmol/min/mg protein, respectively. The benzaldehyde oxidase activity was markedly inhibited by menadione and chlorpromazine. The substrate specificity was different from those of the enzymes from other animals.
Sugihara
K
K
Institute of Pharmaceutical Science, Hiroshima University School of Medicine, Japan.
Katsuma
Y
Y
Tanaka
C
C
Kitamura
S
S
D042931:Aldehyde Oxidase; D000445:Aldehyde Oxidoreductases / Q000302:isolation & purification*; D000818:Animals; D002850:Chromatography, Gel; D006224:Cricetinae; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008647:Mesocricetus; D008970:Molecular Weight; D011506:Proteins / Q000737:chemistry; D011817:Rabbits; D013045:Species Specificity
D011506:Proteins; D000445:Aldehyde Oxidoreductases; D042931:Aldehyde Oxidase