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- W1983162359 abstract "Various methods for studying the IgG interaction with its placental receptor have been examined to establish kinetic parameters. IgG binding has an average rate constant k1 of (2.57 +/- 0.94) x 10(7)/M per min. However, high displacement doses (1000 micrograms) of unlabelled IgG resulted in a curvilinear dissociation curve with two binding sites: one with a fast dissociation rate constant, k2 of 0.100/min and a slow one with k2 of 0.010/min. IgG binding was associated with a high average affinity of (3.70 +/- 1.65) x 10(8)/M and a total number of receptor binding sites of (2.07 +/- 0.93) x 10(14) sites/mg of membrane protein, in close agreement with previous results. The stoichiometry of IgG to Fc gamma-receptor was established as a 4:1 binding ratio from log dose-response curves as opposed to a 1:1 binding ratio from previous reports." @default.
- W1983162359 created "2016-06-24" @default.
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- W1983162359 date "1990-01-01" @default.
- W1983162359 modified "2023-09-29" @default.
- W1983162359 title "A kinetic study of human IgG binding to placental Fcγ-receptor" @default.
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- W1983162359 doi "https://doi.org/10.1016/0161-5890(90)90059-9" @default.
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