An enzyme-linked immunoassay for the collagen cross-link pyridinoline.
نویسنده
چکیده
An inhibition immunoassay method for the determination of pyridinoline was developed with the use of microtitre plates coated with a pyridinoline--gelatin conjugate and rabbit antisera directed against pyridinoline linked to bovine serum albumin. The sensitivity of the assay is about 2pmol of pyridinoline, and the presence of related pyridinium and lysine-derived compounds does not significantly interfere with the procedure. Its application to tissue and human urine samples is described.
منابع مشابه
Measurement of the cross linking compound, pyridinoline, in urine as an index of collagen degradation in joint disease.
An enzyme linked immunoassay (ELISA) for the collagen cross link, pyridinoline, has been developed using affinity purified antibodies, with a sensitivity down to about 0.1 ng of cross link. Measurements of urinary pyridinoline were made in patients with rheumatoid arthritis (RA), osteoarthritis (OA), and a control group showing no signs of joint disease. Expressed relative to creatinine values,...
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BACKGROUND Collagen cross-link molecules such as pyridinoline (PYD), deoxypyridinoline (DPD), and N-terminal cross-linked peptides (NTX) have been measured in urine as indices of bone resorption. However, very little is known regarding the excretion of pyridinolines into other biological fluids. We report a collection device, normalizing analyte, and high-sensitivity immunoassay for quantitativ...
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A component, termed pyridinoline, has been reported to be derived from 'lysine aldehyde' (2,6-diaminohexanaldehyde) and designated as the stable cross-link of mature collagen. Commerically prepared collagen and freshly obtained mature bovine tendon collagen were both investigated with regard to their pyridinoline content. Both sources of material could be depleted of this component by mild wash...
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متن کاملType III collagen, a fibril network modifier in articular cartilage.
The collagen framework of hyaline cartilages, including articular cartilage, consists largely of type II collagen that matures from a cross-linked heteropolymeric fibril template of types II, IX, and XI collagens. In the articular cartilages of adult joints, type III collagen makes an appearance in varying amounts superimposed on the original collagen fibril network. In a study to understand be...
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عنوان ژورنال:
- The Biochemical journal
دوره 207 3 شماره
صفحات -
تاریخ انتشار 1982