Similarity in the aldehyde oxidases from guinea-pig liver and polymorphonuclear leucocytes.
Partially purified enzyme from guinea-pig leucocytes has been shown to have properties similar to both guinea-pig and rabbit liver aldehyde oxidase. The presence of molybdenum in the leucocyte enzyme has been demonstrated and substrate oxidation by either guinea-pig enzyme was found to be completely inhibited by menadione, a potent inhibitor of rabbit liver aldehyde oxidase. The leucocyte enzyme resembles the guinea-pig liver enzyme in terms of substrate specificity but there is considerable variation in substrate oxidation rates between the two species.
Beedham
C
C
D000444:Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D006098:Granulocytes / Q000201:enzymology*; D006168:Guinea Pigs; D008099:Liver / Q000201:enzymology*; D008982:Molybdenum / Q000032:analysis; D010084:Oxidation-Reduction; D013379:Substrate Specificity; D014812:Vitamin K / Q000494:pharmacology
D014812:Vitamin K; D008982:Molybdenum; D000444:Aldehyde Dehydrogenase