Murphy D G, Davidson W S
Int J Biochem. 1986;18(3):215-21. doi: 10.1016/0020-711x(86)90108-4.
An enzyme that catalyzes the NADPH-dependent reduction of a wide range of aromatic and hydroxy-aliphatic aldehydes was purified from chicken breast muscle. This enzyme shares many properties with mammalian aldose reductases including molecular weight, relative substrate specificity, Michaelis constants, an inhibitor specificity. Therefore, it seems appropriate to call this enzyme an aldose reductase (EC 1.1.1.21). Chicken muscle aldose reductase appears to be kinetically identical to an aldose reductase that has been purified from chicken kidney (Hara et al., Eur. J. Biochem. 133, 207-214) and to hen muscle L-glycol dehydrogenase (Bernado et al., Biochim. biophys. Acta 659, 189-198). The association of this aldose reductase with muscular dystrophy in the chick is discussed.
从鸡胸肌中纯化出一种能催化多种芳香族和羟基脂肪族醛类进行依赖于NADPH的还原反应的酶。该酶与哺乳动物醛糖还原酶具有许多共同特性,包括分子量、相对底物特异性、米氏常数及抑制剂特异性。因此,将此酶称为醛糖还原酶(EC 1.1.1.21)似乎是合适的。鸡肌肉醛糖还原酶在动力学上似乎与从鸡肾中纯化出的醛糖还原酶(原田等人,《欧洲生物化学杂志》133卷,207 - 214页)以及母鸡肌肉L - 甘油脱氢酶(贝尔纳多等人,《生物化学与生物物理学报》659卷,189 - 198页)相同。本文讨论了这种醛糖还原酶与雏鸡肌肉萎缩症的关系。