Claims
- 1. A method of analyzing a body fluid sample for the presence of an analyte indicative of type I collagen degradation in vivo, comprising the steps of contacting the body fluid sample with an immunological binding partner which is capable of binding to the analyte, detecting any binding of the immunological binding partner in the body fluid sample, and correlating the detected binding to type I collagen degradation in vivo, wherein the immunological binding partner is capable of binding to a peptide containing a 3-hydroxypyridinium cross-link derived from the carboxy-terminal telopeptide domain of type I collagen, the peptide comprising ##STR14## wherein K--K--K is a 3-hydroxypyridinium cross-link selected from among hydroxylysyl pyridinoline and lysyl pyridinoline, and wherein the immunological binding partner is also capable of binding to the peptide when the pyridinium ring of the 3-hydroxypyridinium cross-link is cleaved.
- 2. The method of claim 1, wherein the analyte is further characterized by having a molecular weight less than 5,000.
- 3. A method of analyzing a body fluid sample for the presence of an analyte indicative of type I collagen degradation in vivo, comprising the steps of contacting the body fluid sample with an immunological binding partner which is capable of binding to the analyte, detecting any binding of the immunological binding partner in the body fluid sample, and correlating the detected binding to type I collagen degradation in vivo, wherein the immunological binding partner is capable of binding to a peptide containing a cleaved pyridinium ring, wherein the peptide is derived by cleavage from a cross-linked peptide containing a 3-hydroxypyridinium cross-link derived from the carboxy-terminal telopeptide domain of type I collagen, the cross-linked peptide comprising ##STR15## wherein K--K--K is a 3-hydroxypyridinium cross-link selected from among hydroxylysyl pyridinoline and lysyl pyridinoline.
- 4. An immunological binding partner that binds to a peptide containing a 3-hydroxypyridinium cross-link derived from the carboxy-terminal telopeptide domain of type I collagen, the peptide consisting of ##STR16## wherein K--K--K is a 3-hydroxypyridinium cross-link selected from among hydroxylysyl pyridinoline and lysyl pyridinoline, and wherein the immunological binding partner also binds to the peptide when the pyridinium ring of the 3-hydroxypyridiniuim cross-link is cleaved.
Parent Case Info
This is a continuation of Ser. No. 08/221,705, filed Apr. 1, 1994, now U.S. Pat. No. 5,473,052, which is a continuation of Ser. No. 07/614,719, filed Nov. 21, 1990, now U.S. Pat. No. 5,300,434, which is a continuation-in-part of Ser. No. 07/444,881, filed Dec. 1, 1989, now U.S. Pat. No. 5,140,103, which is a continuation-in-part of Ser. No. 07/118,234, filed Nov. 6, 1987, now U.S. Pat. No. 4,973,666, the benefits of the filing dates of which are hereby claimed under 3.5 U.S.C. .sctn.120.
Government Interests
This invention was made with government support under one or more grants AM 26489, AR 37318, AM 30774, and AR 36794 awarded by the National Institutes of Health. The government has certain rights in the invention.
US Referenced Citations (9)
Foreign Referenced Citations (1)
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128 041 |
Jun 1983 |
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Continuations (2)
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221705 |
Apr 1994 |
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614719 |
Nov 1990 |
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Continuation in Parts (2)
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444881 |
Dec 1989 |
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118234 |
Nov 1987 |
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