Document Detail

Purification and some properties of hamster liver aldehyde oxidase.
MedLine Citation:
PMID:  10598038     Owner:  NLM     Status:  MEDLINE    
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.
K Sugihara; Y Katsuma; C Tanaka; S Kitamura
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Biological & pharmaceutical bulletin     Volume:  22     ISSN:  0918-6158     ISO Abbreviation:  Biol. Pharm. Bull.     Publication Date:  1999 Nov 
Date Detail:
Created Date:  2000-01-31     Completed Date:  2000-01-31     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9311984     Medline TA:  Biol Pharm Bull     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  1246-8     Citation Subset:  IM    
Institute of Pharmaceutical Science, Hiroshima University School of Medicine, Japan.
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MeSH Terms
Aldehyde Oxidase
Aldehyde Oxidoreductases / isolation & purification*
Chromatography, Gel
Cytosol / enzymology
Electrophoresis, Polyacrylamide Gel
Guinea Pigs
Liver / enzymology*
Molecular Weight
Proteins / chemistry
Species Specificity
Reg. No./Substance:
0/Proteins; EC 1.2.-/Aldehyde Oxidoreductases; EC Oxidase

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