Allen G, Harris J I
Biochem J. 1975 Dec;151(3):747-9. doi: 10.1042/bj1510747.
The binding of NAD+ to glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) from Bacillus stearothermophilus has been studied by measurement of protein fluorescence quenching. Slight negative co-operativity was observed in the binding of the third and fourth coenzyme molecules to the tetrameric enzyme. The first two coenzyme molecules were tightly bound. In this respect the enzyme resembles that from sturgeon muscle rather than that from yeast.
通过测量蛋白质荧光猝灭,研究了NAD⁺与嗜热脂肪芽孢杆菌甘油醛-3-磷酸脱氢酶(EC 1.2.1.12)的结合情况。在第三个和第四个辅酶分子与四聚体酶的结合中观察到轻微的负协同效应。前两个辅酶分子紧密结合。在这方面,该酶类似于鲟鱼肌肉中的酶,而不是酵母中的酶。