Aldehyde dehydrogenase of the Mongolian gerbil, Meriones unguiculatus.
Aldehyde dehydrogenase of the Mongolian gerbil, Meriones unguiculatus.
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蒙古沙鼠（Meriones unguiculatus）的醛脱氢酶。
DOI：
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发表时间：
1979
期刊：
影响因子：
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通讯作者：
R. Lindhal
中科院分区：
文献类型：
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作者：
F. Simpson;R. Lindhal
醛脱氢酶（Aldehyde：NAD（P）oxidoreductase E.C.）1.2.1.3.和1.2.1.5）表型。沙鼠醛脱氢酶的组织分布与大鼠相似，肝脏具有大部分醛脱氢酶活性。雄性肾脏和精巢的活性显著高于雌性肾脏和卵巢。沙鼠肝醛脱氢酶的底物和辅酶特异性也与大鼠和小鼠肝脏相似。凝胶等电聚焦解决一个主要的沙鼠肝醛脱氢酶同工酶在pI 5.3。小鼠肝脏分解为两种主要同工酶，pI为5.3和5.6，大鼠肝脏醛脱氢酶分解为一种主要同工酶，pI为5.4。沙鼠肝醛脱氢酶在较宽的pH范围内具有功能，最适pH为9.0。大鼠和小鼠肝醛脱氢酶具有尖锐的pH最适pH 8.5。
The aldehyde dehydrogenase (Aldehyde:NAD(P) oxidoreductase E.C. 1.2.1.3. and 1.2.1.5) phenotype in several tissues of the Mongolian gerbil, Meriones unguiculatus, has been established. The tissue distribution of gerbil aldehyde dehydrogenase is similar to that of the rat, with liver possessing the majority of the aldehyde dehydrognease activity. Male kidney and testis possess significantly more activity than female kidney and ovary. The substrate and co-enzyme specificity of gerbil liver aldehyde dehydrogenase is also similar to that of rat and mouse liver. Gel isoelectric focusing resolves one major gerbil liver aldehyde dehydrogenase isozyme at pI 5.3. Mouse liver is resolved into two major isozymes at pIs 5.3 and 5.6 and rat liver aldehyde dehydrogenase into one major isozyme at pI 5.4. Gerbil liver aldehyde dehydrogenase is functional over a broad pH range with an optima at pH 9.0. Rat and mouse liver aldehyde dehydrogenase possess sharp pH optima at pH 8.5.