Jacobson K B
Science. 1968 Jan 19;159(3812):324-5. doi: 10.1126/science.159.3812.324.
Isoenzymes of alcohol dehydrogenase extracted from Drosophila melanogaster are interconvertible and can be distinguished by electrophoretic mobility. When adsorbed on diethylaminoethyl cellulose, the faster-moving forms are converted to the slowest-moving form; the latter is converted to the former in the presence of 0.05 molar nicotinamide-adenine dinucleotide, and the conversion is accompanied by the binding of 3.5 moles of the dinucleotide per mole of enzyme. A change in heat stability accompanies the conversion of the slowest form of alcohol dehydrogenase to the fastest form; the latter becomes stable at 45 degrees C. The increased heat stability may indicate that a conformational change in the alcohol dehydrogenase occurs along with the binding of nicotinamide-adenine dinucleotide.
从黑腹果蝇中提取的乙醇脱氢酶同工酶是可相互转化的，并且可以通过电泳迁移率来区分。当吸附在二乙氨基乙基纤维素上时，迁移速度较快的形式会转化为迁移速度最慢的形式；在0.05摩尔烟酰胺腺嘌呤二核苷酸存在的情况下，后者会转化为前者，并且这种转化伴随着每摩尔酶结合3.5摩尔的二核苷酸。乙醇脱氢酶最慢形式向最快形式的转化伴随着热稳定性的变化；最快形式在45摄氏度时变得稳定。热稳定性的增加可能表明乙醇脱氢酶的构象变化与烟酰胺腺嘌呤二核苷酸的结合同时发生。
