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Identification of Strychnine Binding Sites in the Rat Retina
Author(s) -
Schaeffer James M,
Anderson Susanne M
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb00606.x
Subject(s) - strychnine , dissociation constant , taurine , glycine , binding site , retina , chemistry , biochemistry , amino acid , biology , receptor , neuroscience
[ 3 H]Strychnine specifically binds to membrane fractions isolated from rat retinae. The binding is saturable, with an apparent dissociation constant, K D , of 14.3 × 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 [ 3 H]strychnine binding ( K i = 4 × 10 −5 M); no other amino acids endogenously present in the retina inhibited [ 3 H]strychnine binding.