Eckert K, Otto M, Grosse R, Heinrich R, Jacobasch G
Acta Biol Med Ger. 1975;34(4):K 11-7.
By means of circular dichroism measurements in the range from 210-240 nm and 250-300 nm it is shown that conformational changes of the phosphofructokinase from rabbit muscle correlate with the action of effectors on the enzyme. The postulated active and inactive states differ in the secondary structure. Addition of activators causes a conformational change which is interpreted as the transition of the inactive into the active state. At 210-240 nm no reversion could be observed but at 250-300 nm there are some indications for at least partial reversion.
通过在210 - 240纳米和250 - 300纳米范围内进行圆二色性测量表明，兔肌肉磷酸果糖激酶的构象变化与效应物对该酶的作用相关。推测的活性状态和非活性状态在二级结构上有所不同。添加激活剂会引起构象变化，这被解释为从非活性状态向活性状态的转变。在210 - 240纳米处未观察到逆转，但在250 - 300纳米处有一些迹象表明至少存在部分逆转。
