Abstract: A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. Antibodies to a glycated protein have been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune response to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In another embodiment, the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A monoclonal antibody, Serex A93, recognizes peptide linked pyridinoline in Type I bone collagen fragments and can be used to quantitate bone resorption. The hybridoma producing this antibody has been deposited with the American Type Culture Collection, Rockville, Md., under accession number HB-12254. The epitope reactive with the antibody is stable to acid hydrolysis and therefore is not a linear peptide. The antibody recognizes pyridinoline in bound or conjugated form, but not in the free form found in urine. The antibody is useful in immunoassays for determining bone resorption, utilizing body fluids such as urine, saliva, blood, or sweat.

Abstract: A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A monoclonal antibody, Serex A93, recognizes peptide linked pyridinoline in Type I bone collagen fragments and can be used to quantitate bone resorption. The hybridoma producing this antibody has been deposited with the American Type Culture Collection, Rockville, Md., under accession number HB-12254. The epitope reactive with the antibody is stable to acid hydrolysis and therefore is not a linear peptide. The antibody recognizes pyridinoline in bound or conjugated form, but not in the free form found in urine. The antibody is useful in immunoassays for determining bone resorption, utilizing body fluids such as urine, saliva, blood, or sweat.

Abstract: Assays using receptor:reland complexes capable of releasing the reland in the presence of an analyte are described, wherein the reland does not detectably compete with analyte for binding to the receptor. The dissociation constant of the reland and the receptor is such that no appreciable release of reland occurs in the absence of analyte for the receptor. In a preferred embodiment, the association constant of the monomeric reland and the receptor is less than or equal to about 10.sup.5 M, preferably 10.sup.3 to 10.sup.5 M, most preferably 1% or less of the association constant of the analyte and receptor. In a preferred embodiment, the reland is labelled and the amount of analyte bound to the receptor is determined from the amount of labelled reland which is released.

Abstract: A method for assaying for the presence of analyte in a sample based on differential binding affinity involves detecting dissociation of a complex of receptor and ligand in the presence of analyte. The receptor binds the analyte with high affinity and with the ligand with low affinity. The receptor-ligand complex may be formed in situ or may be preformed. In the presence of free analyte, the receptor releases from the receptor-ligand complex and binds free analyte. Release of the receptor-ligand complex is detectable. A kit for performing release assays to detect the presence of analyte is also provided.