Abstract: Immunoassay test kit for detecting analyte indicative of type I collagen resorption in vivo, comprising an immunological binding partner which binds to an amino-terminal or carboxy-terminal 3-hydroxypyridinium cross-linked telopeptide of type I collagen isolatable from a urine sample of a patient with active Paget's disease, wherein the immunological binding partner does not cross-react more than 10% with the type II and type III collagen telopeptides of formulas XVI, XIV, XII, XI, VII, VIII, X, IX, and XI.

Abstract: An immunoassay test kit including an immunological binding partner that binds to lysyl pyridinoline, for analyzing a body fluid sample for bone resorption in vivo.

Abstract: In a method of analyzing a body fluid sample for the presence of analyte indicative of a physiological condition, comprising the steps of contacting the body fluid sample with an immunological binding partner which binds to the analyte, detecting binding of the immunological binding partner to the analyte, and correlating any detected binding to the physiological condition, the improvement comprising contacting the body fluid sample with an immunological binding partner which binds to(Gln)-(Tyr)-(Ser)-(Tyr)-(Asp)-(Val)-Hyl- .vertline. (Gln)-(Tyr)-(Ser)-(Tyr)-(Asp)-(Val)-Hyl- .vertline. (Gly)-Ile-Hyl- -Ser-Gly-Val-Ala-Val-Gly-Gly -Ser-Gly-Val-Ala-Val-Gly-Gly -Gly-His-Argwherein the cross-linking residue depicted as Hyl-Hyl-Hyl is hydroxylysyl pyridinoline and the parentheses indicate optional amino acid residues, and correlating any detected binding to degradation of type III collagen in vivo.

Abstract: Peptides synthesized to match the human .alpha.1(I) and .alpha.2(I) telopeptide sequences of the type I collagen metabolites, preferably selected from among Asp-Glu-Lys-Ser-Thr-Gly-Gly (SEQ ID NO:5), Gln-Tyr-Asp-Gly-Lys-Gly-Val-Gly (SEQ ID NO:6), and Glu-Lys-Ala-His-Asp-Gly-Gly-Arg (SEQ ID NO:7). Useful as calibrators and antigens in immunoassays for detecting type I collagen degradation products in body fluids.

Abstract: Urinary assay for measuring bone resorption, by contacting an unhydrolyzed urine sample with an antibody that binds to free lysyl pyridinoline cross-links, detecting any binding of the antibody in the body fluid sample, and correlating the detected binding to bone resorption in vivo. The free lysyl pyridinoline cross-links are preferably measured as a ratio to the creatinine content in order to provide a urinary index of bone resorption independent of urine volume.

Abstract: A method for assaying bone resorption rates which consists of quantitating the concentration of free lysyl pyridinoline derived from bone collagen, found in a body fluid is disclosed. The method includes immunometric assay, fluorometric assay and electrochemical titration. The structure of specific 3-hydroxypyridinium cross-links found in urine of Paget's disease patients and procedures for making monoclonal antibodies is described.

Abstract: Method of monitoring a patient's response to an anti-resorptive therapy such as estrogen, by contacting a body fluid sample of the patient with an immunological binding partner specific for a cross-linked telopeptide having a sequence identical to that of a cross-linked amino-terminal or carboxy-terminal telopeptide produced in vivo upon degradation of type I collagen, detecting any binding of the immunological binding partner in the body fluid sample, and correlating the detected binding to the rate of bone resorption in the patient.

Abstract: In a method of analyzing a body fluid sample for the presence of an analyte indicative of a physiological condition, comprising the steps of contacting the body fluid sample with an immunological binding partner which binds to the analyte, detecting binding of the immunological binding partner to the analyte, and correlating any detected binding to the physiological condition, the improvement comprising contacting the body fluid sample with an immunological binding partner which binds to ##STR1## wherein ##STR2## is hydroxylysyl pyridinoline or lysyl pyridinoline, and correlating any detected binding to degradation of type II collagen in vivo.

Abstract: Compositions useful in quantitating collagen peptides to determine the rate of bone resorption are prepared by treating bone with a protease, such as collagenase, and purifying the compositions so as to enrich them with peptides that contain 3-hydroxypyridinium cross-links.

Abstract: A method of determining collagen degradation in vivo, comprising quantitating the concentration of a peptide in a body fluid, the peptide being a C-terminal type II collagen telopeptide containing a hydroxylysyl pyridinoline cross-link or a type III collagen telopeptide containing a hydroxylysyl pyridinoline cross-link. The method includes immunometric assays, fluorometric assays, and electrochemical titrations for quantitation. The structures of specific peptides having cross-links and kits for quantitating these peptides in a body fluid are described.

Abstract: Synthetic linear peptides embodied by Xaa-Tyr-Xaa-Gly-Xaa-Gly-Val-Gly which mimic the epitope recognized by mAb 1H11 (ATCC No. HB 10611) in cross-linked N-telopeptides of type I collagen (NTx).

Abstract: Synthetic linear peptides embodied by Y-Tyr-Asp-Gly-X-Gly-Val-Gly (SEQ ID NO:1) which mimic the epitope recognized by mAb 1H11 (ATCC No. HB 10611) in cross-linked N-telopeptides of type I collagen (NTx).

Abstract: In a method of analyzing a body fluid sample for the presence of an analyte indicative of a physiological condition, comprising the steps of contacting the body fluid sample with an immunological binding partner which binds to the analyte, detecting binding of the immunological binding partner to the analyte, and correlating any detected binding to the physiological condition, the improvement comprising contacting the body fluid sample with an immunological binding partner which binds to ##STR1## wherein ##STR2## is hydroxylysyl pyridinoline or lysyl pyridinoline, and correlating any detected binding to degradation of type II collagen in vivo.

Abstract: Methods of determining collagen degradation in vivo, by quantitating the concentration of a peptide in a body fluid, the peptide having the following structure: ##STR1## is hydroxylysyl pyridinoline or lysyl pyridinoline, and J is pyroglutamic acid or glutamine and (Leu) are optional leucines, are disclosed.

Abstract: Methods of determining collagen degradation in vivo, by quantitating the concentration of a peptide in a body fluid, the peptide being a C-terminal type II collagen telopeptide containing a hydroxylysyl pyridinoline cross-link or a type III collagen telopeptide containing a hydroxylysyl pyridinoline cross-link. Suitable methods include immunometric assays, fluorometric assays, and electrochemical titrations for quantitation. The structures of specific peptides having cross-links and kits for quantitating these peptides in a body fluid are described.

Abstract: Methods of determining collagen degradation in vivo, by quantitating the concentration of a peptide in a body fluid, the peptide being a C-terminal type II collagen telopeptide containing a hydroxylysyl pyridinoline cross-link or a type III collagen telopeptide containing a hydroxylysyl pyridinoline cross-link. Suitable methods include immunometric assays, fluorometric assays, and electrochemical titrations for quantitation. The structures of specific peptides having cross-links and kits for quantitating these peptides in a body fluid are described.

Abstract: A method of determining collagen degradation in vivo, comprising quantitating the concentration of a peptide in a body fluid, the peptide being a C-terminal type II collagen telopeptide containing a hydroxylysyl pyridinoline cross-link or a type III collagen telopeptide containing a hydroxylysyl pyridinoline cross-link. The method includes immunometric assays, fluorometric assays, and electrochemical titrations for quantitation. The structures of specific peptides having cross-links and kits for quantitating these peptides in a body fluid are described.

Abstract: A method of determining collagen degradation in vivo, comprising quantitating the concentration of a peptide in a body fluid, the peptide being a C-terminal type II collagen telopeptide containing a hydroxylysyl pyridinoline cross-link or a type III collagen telopeptide containing a hydroxylysyl pyridinoline cross-link. The method includes immunometric assays, fluorometric assays, and electrochemical titrations for quantitation. The structures of specific peptides having cross-links and kits for quantitating these peptides in a body fluid are described.

Abstract: A method of determining collagen degradation in vivo, comprising quantitating the concentration of a peptide in a body fluid, the peptide being a C-terminal type II collagen telopeptide containing a hydroxylysyl pyridinoline cross-link or a type III collagen telopeptide containing a hydroxylysyl pyridinoline cross-link. The method includes immunometric assays, fluorometric assays, and electrochemical titrations for quantitation. The structures of specific peptides having cross-links and kits for quantitating these peptides in a body fluid are described.

Abstract: A method for assaying bone resorption rates which consists of quantitating the concentration of peptide fragments derived from bone collagen, found in a body fluid is disclosed. The method includes immunometric assay, fluorometric assay and electrochemical titration. The structure of specific peptide fragments having 3-hydroxypyridinium cross-links found in urine of Paget's disease patients and procedures for making monoclonal antibodies is described.