Kazarov A R, Rozenkrants A A, Sobolev A S
Biull Eksp Biol Med. 1988 Sep;106(9):319-21.
Variations in the intrinsic activity of 1-isoproterenol and in the percentage of high affinity beta-receptor complexes have been studied under a changes in the macrostructure of reticulocyte plasma membranes. The fluid lipid fraction have been reduced in the membranes for this by phospholipase A2/BSA treatment. It was accompanied by a progressive decrease in the fraction of beta-receptors that are able to form the high affinity complexes with 1-isoproterenol (receptor--regulatory N-protein complexes). Evaluated with the ability to activate the adenylate cyclase, the intrinsic activity of 1-isoproterenol was decreased from 1 to 0 under with conditions. This variations proved to correlate strongly with each other. Thus, changes in the membrane macrostructure may directly determine an efficiency of hormone actions.
在网织红细胞质膜宏观结构发生变化的情况下,研究了1-异丙肾上腺素的内在活性变化以及高亲和力β受体复合物的百分比。为此,通过磷脂酶A2/牛血清白蛋白处理使膜中的流动性脂质部分减少。这伴随着能够与1-异丙肾上腺素形成高亲和力复合物的β受体部分(受体 - 调节性N蛋白复合物)的逐渐减少。用激活腺苷酸环化酶的能力评估,在这些条件下1-异丙肾上腺素的内在活性从1降至0。事实证明,这些变化彼此密切相关。因此,膜宏观结构的变化可能直接决定激素作用的效率。