Cynomolgus monkey liver aldehyde oxidase: extremely high oxidase activity and an attempt at purification

Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology Pub Date : 2000-05-01 DOI:10.1016/S0742-8413(00)00095-5

Kazumi Sugihara , Yasuko Katsuma , Shigeyuki Kitamura , Shigeru Ohta , Morioki Fujitani , Hideaki Shintani

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引用次数: 13

Abstract

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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食蟹猴肝醛氧化酶:氧化酶活性极高，并尝试提纯

对猕猴肝脏中的醛氧化酶(EC 1.2.3.1)进行了表征。与家兔、大鼠、小鼠和豚鼠相比，肝细胞质中苯甲醛和酞菁氧化酶活性极高。猴肝醛氧化酶具有广泛的底物特异性，与其他哺乳动物的酶不同。猴肝细胞质中纯化的醛氧化酶在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)中显示出两条主要带和两条次要带。用抗大鼠醛氧化酶进行免疫印迹分析，也观察到这些条带。SDS-PAGE测定酶的分子量为130-151 kDa, HPLC凝胶过滤测定酶的分子量为285 kDa。结果表明，猴肝脏中存在乙醛氧化酶同工型。

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Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology

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