Abstract
Immunogobulin G fractions prepared from conventional rabbit anti-thyroxine (T 4) antisera were fractionated by agarose gel isoelectric focusing (IEF) in the range of pH 3 to 10, and by chromatofocusing using a Fast Protein Liquid Chromatography (FPLC) system. The clonotype antibodies were recovered from the fractions and subjected to Scatchard plot anlysis. The highest affinity constants of the initial antibody (shown in parentheses) and those of the antibodies recovered were IEF, 1.8 × 10 9 to 8.3 × 10 9 m −1(2.2 × 10 9 m −1); FPLC, 2.4 × 10 9 to 6.0 × 10 9 m −1 (2.5 × 10 9 m −1). A sensitive radioimmunoassay of T 4 was achieved with the isolated high-affinity anti-T 4 antibody. The minimum detectable concentration of T 4 was 6.3 × 10 −15 to 1.5 × 10 −14 mol/tube, which was three to five times lower than that detectable with the initial antibodies.
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