Schaeffer J M, Anderson S M
J Neurochem. 1981 Apr;36(4):1597-600. doi: 10.1111/j.1471-4159.1981.tb00606.x.
[3H]Strychnine specifically binds to membrane fractions isolated from rat retinae. The binding is saturable, with an apparent dissociation constant, KD, of 14.3 x 10(-9) M and 205 fmol bound/mg protein. Specific binding is time-dependent and proportional to protein concentration. Glycine and taurine are equally potent inhibitors of [3H]strychnine binding (Ki = 4 x 10(-5) M); no other amino acids endogenously present in the retina inhibited [3H]strychnine binding.
[3H]士的宁特异性结合从大鼠视网膜分离的膜组分。这种结合是可饱和的，表观解离常数KD为14.3×10⁻⁹ M，结合量为205 fmol/mg蛋白质。特异性结合具有时间依赖性，且与蛋白质浓度成正比。甘氨酸和牛磺酸是[3H]士的宁结合的同等强效抑制剂（Ki = 4×10⁻⁵ M）；视网膜中内源性存在的其他氨基酸均不抑制[3H]士的宁结合。
