洛菲不动杆菌的异柠檬酸脱氢酶。两种烟酰胺腺嘌呤二核苷酸磷酸连接的同工酶的分离及性质
The isocitrate dehydrogenases of Acinetobacter lwoffi. Separation and properties of two nicotinamide-adenine dinucleotide phosphate-linked isoenzymes.
作者信息
Self C H, Weitzman P D
出版信息
Biochem J. 1972 Nov;130(1):211-9. doi: 10.1042/bj1300211.
Abstract
Two isoenzymes of NADP-linked isocitrate dehydrogenase have been identified in Acinetobacter lwoffi and have been termed isoenzyme-I and isoenzyme-II. The isoenzymes may be separated by ion-exchange chromatography on DEAE-cellulose, by gel filtration on Sephadex G-200, or by zonal ultracentrifugation in a sucrose gradient. Low concentrations of glyoxylate or pyruvate effect considerable stimulation of the activity of isoenzyme-II. The isoenzymes also differ in pH-dependence of activity, kinetic parameters, stability to heat or urea and molecular size. Whereas isoenzyme-I resembles the NADP-linked isocitrate dehydrogenases from other organisms in having a molecular weight under 100000, isoenzyme-II is a much larger enzyme (molecular weight around 300000) resembling the NAD-linked isocitrate dehydrogenases of higher organisms.
摘要
已在洛菲不动杆菌中鉴定出两种与NADP相关的异柠檬酸脱氢酶同工酶，分别称为同工酶-I和同工酶-II。这些同工酶可通过在DEAE-纤维素上进行离子交换色谱、在Sephadex G-200上进行凝胶过滤或在蔗糖梯度中进行区带超速离心来分离。低浓度的乙醛酸或丙酮酸对同工酶-II的活性有显著的刺激作用。这些同工酶在活性的pH依赖性、动力学参数、对热或尿素的稳定性以及分子大小方面也存在差异。同工酶-I的分子量低于100000，类似于其他生物中与NADP相关的异柠檬酸脱氢酶，而异工酶-II是一种大得多的酶（分子量约为300000），类似于高等生物中与NAD相关的异柠檬酸脱氢酶。
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