Young A B, Snyder S H
Proc Natl Acad Sci U S A. 1973 Oct;70(10):2832-6. doi: 10.1073/pnas.70.10.2832.
[(3)H]Strychnine binds to synaptic-membrane fractions of the spinal cord in a selective fashion, indicating an interaction with postsynaptic glycine receptors. Displacement of strychnine by glycine and other amino acids parallels their glycine-like neurophysiologic activity. The regional localization of strychnine binding in the central nervous system correlates closely with endogenous glycine concentrations. In subcellular fractionation experiments, strychnine binding is most enhanced in synaptic-membrane fractions. Strychnine binding is saturable, with affinity constants for glycine and strychnine of 10 and 0.03 muM, respectively.
[(3)H]士的宁以一种选择性方式与脊髓的突触膜部分结合,表明其与突触后甘氨酸受体相互作用。甘氨酸和其他氨基酸对士的宁的取代作用与其类似甘氨酸的神经生理活性平行。士的宁在中枢神经系统中的结合区域定位与内源性甘氨酸浓度密切相关。在亚细胞分级分离实验中,突触膜部分的士的宁结合增强最为明显。士的宁结合具有饱和性,甘氨酸和士的宁的亲和常数分别为10和0.03μM。