PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8404825-4 1993 Bound IgE was demonstrated by autoradiography using 125I-labeled anti-human IgE. Iodine-125 52-56 immunoglobulin heavy constant epsilon Homo sapiens 6-9 8404825-4 1993 Bound IgE was demonstrated by autoradiography using 125I-labeled anti-human IgE. Iodine-125 52-56 immunoglobulin heavy constant epsilon Homo sapiens 76-79 2434548-3 1987 After incubation of human sera with these disks or bovine serum albumin substituted disks as a control, the binding of IgE was assessed with 125I-labeled antihuman IgE. Iodine-125 141-145 immunoglobulin heavy constant epsilon Homo sapiens 119-122 2523671-3 1989 A 100-fold excess of monoclonal anti-IgE antibodies inhibited binding of 125I labeled IgE to Fc epsilon RII on Wil-2WT cells. Iodine-125 73-77 immunoglobulin heavy constant epsilon Homo sapiens 37-40 2523671-3 1989 A 100-fold excess of monoclonal anti-IgE antibodies inhibited binding of 125I labeled IgE to Fc epsilon RII on Wil-2WT cells. Iodine-125 73-77 immunoglobulin heavy constant epsilon Homo sapiens 86-89 3584974-5 1987 The RNA was capable of binding allergen-specific IgE in sera from two shrimp-sensitive patients, as demonstrated by microELISA and solid-phase radioimmunoassay (SPRIA) using antigen-coated nitrocellulose filter paper discs and purified 125I-labeled goat anti-human IgE. Iodine-125 236-240 immunoglobulin heavy constant epsilon Homo sapiens 49-52 422286-2 1979 These were used to construct a calibration curve for the subsequent binding of 125I-labelled anti-IgE, thus relating 125I counts to WHO IgE units. Iodine-125 79-83 immunoglobulin heavy constant epsilon Homo sapiens 98-101 6833769-2 1983 Binding of 125I-labeled B5 was specific for rat IgE and did not crossreact with human IgE. Iodine-125 11-15 immunoglobulin heavy constant epsilon Homo sapiens 48-51 761393-2 1979 By replacing the 125I-labelled anti-IgE antibody used in the paper radioimmunosorbent test by the 125I-labelled anti-IgE reagent used in radioallergosorbent test (RAST) and by changing the serum dilution and the incubation time, this modified sandwich technique (MST) became comparable to the RIST in the normal and elevated IgE-region and showed results similar to the PRIST in the very low IgE-region. Iodine-125 17-21 immunoglobulin heavy constant epsilon Homo sapiens 36-39 761393-2 1979 By replacing the 125I-labelled anti-IgE antibody used in the paper radioimmunosorbent test by the 125I-labelled anti-IgE reagent used in radioallergosorbent test (RAST) and by changing the serum dilution and the incubation time, this modified sandwich technique (MST) became comparable to the RIST in the normal and elevated IgE-region and showed results similar to the PRIST in the very low IgE-region. Iodine-125 98-102 immunoglobulin heavy constant epsilon Homo sapiens 117-120 761393-2 1979 By replacing the 125I-labelled anti-IgE antibody used in the paper radioimmunosorbent test by the 125I-labelled anti-IgE reagent used in radioallergosorbent test (RAST) and by changing the serum dilution and the incubation time, this modified sandwich technique (MST) became comparable to the RIST in the normal and elevated IgE-region and showed results similar to the PRIST in the very low IgE-region. Iodine-125 98-102 immunoglobulin heavy constant epsilon Homo sapiens 117-120 761393-2 1979 By replacing the 125I-labelled anti-IgE antibody used in the paper radioimmunosorbent test by the 125I-labelled anti-IgE reagent used in radioallergosorbent test (RAST) and by changing the serum dilution and the incubation time, this modified sandwich technique (MST) became comparable to the RIST in the normal and elevated IgE-region and showed results similar to the PRIST in the very low IgE-region. Iodine-125 98-102 immunoglobulin heavy constant epsilon Homo sapiens 117-120 761393-3 1979 The affinity of the 125I-labelled anti-IgE of the RAST proved to be about 2.6 times higher than the antibody used in the PRIST, which explains the improved results in the normal and the good results in the very low IgE-region. Iodine-125 20-24 immunoglobulin heavy constant epsilon Homo sapiens 39-42 761393-3 1979 The affinity of the 125I-labelled anti-IgE of the RAST proved to be about 2.6 times higher than the antibody used in the PRIST, which explains the improved results in the normal and the good results in the very low IgE-region. Iodine-125 20-24 immunoglobulin heavy constant epsilon Homo sapiens 215-218 2433321-2 1987 Fifteen percent of the 288 spice RASTs resulted in greater than or equal to 10% binding of 125I-labeled anti-IgE. Iodine-125 91-95 immunoglobulin heavy constant epsilon Homo sapiens 109-112 7119454-2 1982 Allergenic proteins were then identified by successive incubation of the transfer membrane with serum from allergic individuals and with 125I-labelled anti-human IgE, followed by autoradiography. Iodine-125 137-141 immunoglobulin heavy constant epsilon Homo sapiens 162-165 422286-2 1979 These were used to construct a calibration curve for the subsequent binding of 125I-labelled anti-IgE, thus relating 125I counts to WHO IgE units. Iodine-125 79-83 immunoglobulin heavy constant epsilon Homo sapiens 136-139 965104-5 1976 Cross-reaction between reaginic bovine antibody and human IgE was shown by a binding assay involving the uptake of 125I-labelled anti-human IgE globulin by mast cells incubated with bovine passive cutaneous anaphylaxis positive globulin. Iodine-125 115-119 immunoglobulin heavy constant epsilon Homo sapiens 58-61 965104-5 1976 Cross-reaction between reaginic bovine antibody and human IgE was shown by a binding assay involving the uptake of 125I-labelled anti-human IgE globulin by mast cells incubated with bovine passive cutaneous anaphylaxis positive globulin. Iodine-125 115-119 immunoglobulin heavy constant epsilon Homo sapiens 140-143 51010-5 1975 Autoradiographic studies with 125I-labelled human serum proteins demonstrated the selective formation of grains on mast cells incubated with labelled IgE. Iodine-125 30-34 immunoglobulin heavy constant epsilon Homo sapiens 150-153