Syva Company

Richard K Leute

Edwin F Ullman

Avram Goldstein

Kenneth E Rubenstein

Judith I Blakemore

Roberta D Ernst

Gunner Bolz

Nitrogen derivatives of benzoyl ecgonine and cocaine are provided, particularly amino, diazonium, and diazo derivatives, the compounds finding use either directly or as intermediates for the preparation of reagents for use in immunoassays. Diazo compounds can be coupled with antigenic materials for the preparation of antibodies to benzoyl ecgonine and/or cocaine. The amino group can be combined with active non-oxo-carbonyl compounds to form reagents which find use in immunoassays.

Antibodies to nitrogen derivatives of benzoyl ecgonine antigenic

An enzyme-polyidothyronine conjugate for use in determining polyiodothyronine by immunoassay is prepared containing an enzyme which is reversibly deactivated by polyiodothyronine and is reactivated by an antibody binding to the polyiodothyronine of the conjugate. Preferred enzymes are malate dehydrogenase and triose phosphate isomerase.

Enzyme-bound-polyidothyronine

A method is provided for the determination of receptors, particularly antibodies, where a polyepitopic reagent is employed, at least one of the epitopes being specific for the receptor of interest. The epitopic sites are situated on the reagent, so that the binding of the receptor of interest to the reagent will sterically hinder binding of receptors other than the receptor of interest. In carrying out the assay, the sample suspected of containing the receptor of interest, the reagent, and a predetermined amount of receptors for the other epitopes are combined. Because of the steric inhibition to the simultaneous binding of the two different receptors, the amount of receptor of interest bound to the reagent will affect the amount of the other receptor which becomes bound to the reagent. By analyzing directly or indirectly for the amount of the receptor which is added in a predetermined amount, and comparing the results to known standards, qualitative or quantitative determinations of the amount of receptor of interest may be made. Various detector systems may be employed for determining the amount of the receptor of interest which is present in the unknown sample. The systems include stable free radicals, enzymes, radioactive labels, fluorescers, and the like.

Receptor steric hindrance immunoassay for receptor determination

Method and enzyme conjugates are provided for determining physiological amounts of polyiodothyronine in physiological fluid, particularly serum. A homogeneous enzyme immunoassay is provided employing an enzyme-bound-polyiodothyronine having less than about 50 percent of the original enzyme activity, whose activity increases upon binding with a receptor. The enzyme-bound-polyiodothyronine, the unknown suspected to containing a polyiodothyronine, and receptor for the polyiodothyronine are combined in an aqueous medium containing substrate for said enzyme and the enzymatic activity of the solution determined. By comparing the result obtained with results obtained from standards having known amounts of polyiodothyronine, the amount of polyiodothyroninein the unknown can be determined. The enzyme-bound-polyiodothyronine employs an enzyme which is reversibly deactivated by polyiodothyronine, so as to be reactived by receptor binding to the polyiodothyronine. Particular enzymes include malate dehydrogenase and triose phosphate isomerase.

Polyiodothyronine immunoassay

Novel compounds are provided which are derivatives of 1,2-diphenyl-3-methyl-4-dimethylamino-2-butanol. The indicated alcohol is employed to prepare the monoester of a dibasic acid which is conjugated with an antigen for the production of antibodies which recognize both propoxyphene and its N-desmethyl metabolite in immunoassays.

Polypeptide propoxyphene derivatives for immunoassay reagents

Compounds are provided for use in assays of organic compounds, where organic compounds of biological interest are determined at extremely low concentrations by combining in a medium, the composition to be determined, hereinafter referred to as ligand, a high molecular weight material of at least 10,000 molecular weight, which has a site spatially characteristic of the ligand, hereinafter referred to as receptor, and an analog of the ligand having a free radical functionality, hereinafter referred to as 'ligand analog'. The ligand analog and ligand in the medium compete for the receptor site, the amount of ligand analog bound to the receptor, being dependent on the amount of ligand present in the medium. By following the change in electron spin resonance spectrum of the ligand analog and comparing it to the change in spectrum which would be obtained in the absence of any ligand, the amount of ligand can be determined.

Ligand determination of spin labeled compounds by receptor

Spin labeled compounds

Compounds are provided for use in assays of organic compounds, where organic compounds of biological interest are determined at extremely low concentrations by combining in a medium, the composition to be determined, hereinafter referred to as ligand, a high molecular weight material of at least 10,000 molecular weight, which has a site spatially characterisitc of the ligand, hereinafter referred to as receptor, and an analog of the ligand having a free radical functionality hereinafter referred to as 'ligand analog'. The ligand analog and ligand in the medium compete for the receptor site, the amount of ligand analog bound to the receptor, being dependent on the amount of ligand present in the medium. By following the change in electron spin resonance spectrum of the ligand analog and comparing it to the change in spectrum which would be obtained in the absence of any ligand, the amount of ligand can be determined.

Ligand determination of spin labeled compounds by receptor displacement

A novel immunoassay is provided, as well as particular reagents, for determining the presence of a ligand. A Reagent is employed having at least two epitopes, one of the epitopes being common with the ligand, and the other epitopes being foreign to the ligand. The two epitopes are positioned in the Reagent so that antibody bound to one of the epitopes sterically inhibits the binding of antibody to the second epitope. In carrying out the assay, the sample, the Reagent, and antibodies to the two epitopes are combined. Because of the steric inhibition to the simultaneous binding of the two antibodies to the Reagent, the amount of antibody bound to the epitope of the Reagent foreign to the ligand will be related to the amount of ligand present in the assay medium. By analyzing directly or indirectly for the antibody bound to the epitope foreign to the ligand, and comparing the results to known standards, qualitative or quantitative determinations of the amount of ligand may be made. Various detector systems may be employed for determining the amount of antibody to the foreign epitope which is unbound or bound. These systems include stable free radicals, enzymes, radioactive labels, fluorescers, and the like.

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Sunnyvale, CA, United States of America

Richard K Leute