{"title":"食蟹猴肝醛氧化酶:氧化酶活性极高，并尝试提纯","authors":"Kazumi Sugihara , Yasuko Katsuma , Shigeyuki Kitamura , Shigeru Ohta , Morioki Fujitani , Hideaki Shintani","doi":"10.1016/S0742-8413(00)00095-5","DOIUrl":null,"url":null,"abstract":"<div><p>Aldehyde oxidase (EC 1.2.3.1) in monkey (<em>Macaca fascicularis</em>) liver was characterized. Liver cytosol exhibited extremely high benzaldehyde and phthalazine oxidase activities based on aldehyde oxidase, compared with those of rabbits, rats, mice and guinea pigs. Monkey liver aldehyde oxidase showed broad substrate specificity distinct from that of the enzyme from other mammals. Purified aldehyde oxidase from monkey liver cytosol showed two major bands and two minor bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These bands were also observed in Western blotting analysis using anti-rat aldehyde oxidase. The molecular mass of the enzyme was estimated to be 130–151 kDa by SDS-PAGE, and to be about 285 kDa by HPLC gel filtration. The results suggest that isoforms of aldehyde oxidase exist in monkey livers.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2000-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00095-5","citationCount":"13","resultStr":"{\"title\":\"Cynomolgus monkey liver aldehyde oxidase: extremely high oxidase activity and an attempt at purification\",\"authors\":\"Kazumi Sugihara , Yasuko Katsuma , Shigeyuki Kitamura , Shigeru Ohta , Morioki Fujitani , Hideaki Shintani\",\"doi\":\"10.1016/S0742-8413(00)00095-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Aldehyde oxidase (EC 1.2.3.1) in monkey (<em>Macaca fascicularis</em>) liver was characterized. Liver cytosol exhibited extremely high benzaldehyde and phthalazine oxidase activities based on aldehyde oxidase, compared with those of rabbits, rats, mice and guinea pigs. Monkey liver aldehyde oxidase showed broad substrate specificity distinct from that of the enzyme from other mammals. Purified aldehyde oxidase from monkey liver cytosol showed two major bands and two minor bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These bands were also observed in Western blotting analysis using anti-rat aldehyde oxidase. The molecular mass of the enzyme was estimated to be 130–151 kDa by SDS-PAGE, and to be about 285 kDa by HPLC gel filtration. The results suggest that isoforms of aldehyde oxidase exist in monkey livers.</p></div>\",\"PeriodicalId\":10586,\"journal\":{\"name\":\"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00095-5\",\"citationCount\":\"13\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0742841300000955\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0742841300000955","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Cynomolgus monkey liver aldehyde oxidase: extremely high oxidase activity and an attempt at purification
Aldehyde oxidase (EC 1.2.3.1) in monkey (Macaca fascicularis) liver was characterized. Liver cytosol exhibited extremely high benzaldehyde and phthalazine oxidase activities based on aldehyde oxidase, compared with those of rabbits, rats, mice and guinea pigs. Monkey liver aldehyde oxidase showed broad substrate specificity distinct from that of the enzyme from other mammals. Purified aldehyde oxidase from monkey liver cytosol showed two major bands and two minor bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These bands were also observed in Western blotting analysis using anti-rat aldehyde oxidase. The molecular mass of the enzyme was estimated to be 130–151 kDa by SDS-PAGE, and to be about 285 kDa by HPLC gel filtration. The results suggest that isoforms of aldehyde oxidase exist in monkey livers.
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