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食蟹猴肝脏醛氧化酶:极高的氧化酶活性及纯化尝试。

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

作者信息

Sugihara K, Katsuma Y, Kitamura S, Ohta S, Fujitani M, Shintani H

机构信息

Institute of Pharmaceutical Science, Hiroshima University School of Medicine, Japan.

出版信息

Comp Biochem Physiol C Toxicol Pharmacol. 2000 May;126(1):53-60. doi: 10.1016/s0742-8413(00)00095-5.

DOI:10.1016/s0742-8413(00)00095-5
PMID:11048665
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.

摘要

对猕猴(食蟹猴)肝脏中的醛氧化酶(EC 1.2.3.1)进行了特性分析。与兔、大鼠、小鼠和豚鼠相比,基于醛氧化酶,肝脏胞质溶胶表现出极高的苯甲醛和酞嗪氧化酶活性。猕猴肝脏醛氧化酶显示出与其他哺乳动物的该酶不同的广泛底物特异性。从猕猴肝脏胞质溶胶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)中显示出两条主要条带和两条次要条带。在使用抗大鼠醛氧化酶的蛋白质印迹分析中也观察到了这些条带。通过SDS-PAGE估计该酶的分子量为130 - 151 kDa,通过高效液相色谱凝胶过滤估计约为285 kDa。结果表明醛氧化酶同工型存在于猕猴肝脏中。

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