细菌烟酰胺腺嘌呤二核苷酸磷酸特异性异柠檬酸脱氢酶的电泳异质性
Electrophoretic heterogeneity of bacterial nicotinamide adenine dinucleotide phosphate-specific isocitrate dehydrogenases.
作者信息
Rowe J J, Reeves H C
出版信息
J Bacteriol. 1971 Nov;108(2):824-7. doi: 10.1128/jb.108.2.824-827.1971.
Abstract
The specific activities of the nicotinamide adenine dinucleotide phosphate-dependent isocitrate dehydrogenase in crude cell-free extracts of 15 different microorganisms, grown aerobically in simple mineral salts media containing glucose as the sole carbon source, ranged from a maximum of 0.820 in Pseudomonas aeruginosa to a minimum of 0.145 in Thiobacillus novellus. Polyacrylamide gel electrophoresis indicated that the bacterial species studied contained electrophoretically distinct proteins exhibiting isocitrate dehydrogenase activity. The electrophoretic mobilities, as well as the differences in stability of the enzyme observed in this study, indicate that the physical and chemical properties of isocitrate dehydrogenase may differ widely between bacterial species.
摘要
在以葡萄糖作为唯一碳源的简单无机盐培养基中需氧培养的15种不同微生物的无细胞粗提物中，烟酰胺腺嘌呤二核苷酸磷酸依赖性异柠檬酸脱氢酶的比活性范围为，铜绿假单胞菌中的最高值0.820至新型硫杆菌中的最低值0.145。聚丙烯酰胺凝胶电泳表明，所研究的细菌种类含有表现出异柠檬酸脱氢酶活性的电泳性质不同的蛋白质。本研究中观察到的电泳迁移率以及酶稳定性的差异表明，不同细菌种类的异柠檬酸脱氢酶的物理和化学性质可能有很大差异。
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