Kaklij G S, Kelkar S M
Biochem Int. 1983 Jan;6(1):43-52.
The effect of phosphorylation of bovine erythrocyte membrane on association of Fructose 1,6-diphosphate (FDP) aldolase has been investigated. The phosphorylation of the membrane seemed to favour the increased association of the enzyme. With the native and NaCl-depleted membrane, it was observed that the extent of phosphorylation could be correlated with the enzyme association. The experiments with the intact erythrocytes isolated from bovine and rabbit blood employing similar conditions, confirmed these findings. The observations with the membrane and whole cells have been substantiated using [gamma-32P]ATP and [32P] inorganic phosphate. The treatment of the enzyme favouring phosphorylation, did not show association of the enzyme with the membrane. The chemical modification of the membrane, influencing the association of the enzyme could be a possible mechanism for fine regulatory control of the activity.
已对牛红细胞膜磷酸化对1,6 - 二磷酸果糖（FDP）醛缩酶结合的影响进行了研究。膜的磷酸化似乎有利于该酶结合增加。对于天然膜和去除NaCl的膜，观察到磷酸化程度与酶结合相关。使用类似条件对从牛血和兔血中分离出的完整红细胞进行的实验证实了这些发现。使用[γ-32P]ATP和[32P]无机磷酸盐证实了对膜和全细胞的观察结果。有利于磷酸化的酶处理未显示该酶与膜的结合。影响酶结合的膜化学修饰可能是对活性进行精细调节控制的一种可能机制。
