大鼠和人类小脑中[3H]红藻氨酸结合位点的协同相互作用。

Cooperative interactions at [3H]kainic acid binding sites in rat and human cerebellum.

作者信息

London E D, Coyle J T

出版信息

Eur J Pharmacol. 1979 Jun 15;56(3):287-90. doi: 10.1016/0014-2999(79)90186-9.

Abstract

Inhibition of the specific binding of [3H]kainic acid was studied in membranes isolated from rat and human cerebellum; the sequence of potencies in both species were: kainic acid greater than L-glutamic acid greater than dihydrokainic acid greater than D-glutamic acid. Whereas the Hill coefficient for unlabelled Kainate was 1.0, dihydrokainic acid and D- and L-glutamic acids exhibited negative cooperativity with Hill coefficients of near 0.5. This allosteric interaction of glutamic acid at the kainic acid recognition site suggests a biochemical correlate for the synergistic effects of these compounds in vivo.

摘要

研究了从大鼠和人类小脑中分离出的膜对[3H]红藻氨酸特异性结合的抑制作用；在这两个物种中，效力顺序为：红藻氨酸＞L-谷氨酸＞二氢红藻氨酸＞D-谷氨酸。未标记红藻氨酸盐的希尔系数为1.0，而二氢红藻氨酸以及D-和L-谷氨酸表现出负协同性，希尔系数接近0.5。谷氨酸在红藻氨酸识别位点的这种变构相互作用表明了这些化合物在体内协同作用的生化相关性。