Triton X-100 eliminates plasma proteins interference in a radioimmunoassay for luteinizing hormone-releasing hormone (LHRH) and LHRH analogues.
A method is described for the radioimmunoassay of native LHRH and DTrp6-LHRH, an LHRH analogue which does not require extraction of plasma samples. Interference by binding proteins normally present in plasma is removed by addition of Triton X-100 to the binding buffer at a concentration of 1% for LHRH and 0.15% for the LHRH analogue. This approach permits a direct estimation of the peptide level in unextracted plasma with quantitative recoveries for concentrations ranging from 0.015 to 10 ng/ml. Although the antiserum titre is reduced, the affinity of the antibody does not change at the detergent concentrations used in this study. This procedure is recommended for peptide assays in which the non-specific effects of plasma prevent a direct assay.
Ezan
E
E
INSERM U.207, Institut Pasteur, URIA, Paris, France.
Drieu
K
K
Dray
F
F
D000818:Animals; D001798:Blood Proteins / Q000032:analysis*; D007987:Gonadotropin-Releasing Hormone / Q000097:blood*; D006801:Humans; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology*; D011863:Radioimmunoassay / Q000379:methods; D051381:Rats; D017329:Triptorelin Pamoate
D001798:Blood Proteins; D017329:Triptorelin Pamoate; D007987:Gonadotropin-Releasing Hormone; D011092:Polyethylene Glycols; D017830:Octoxynol