Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Clinical Chemistry 45: 682-683, 1999;
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Web of Science (3)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Traba, M. L.
Right arrow Articles by de la Piedra, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Traba, M. L.
Right arrow Articles by de la Piedra, C.
Related Collections
Right arrow Proteomics and Protein Markers
Right arrow Endocrinology and Metabolism
(Clinical Chemistry. 1999;45:682-683.)
© 1999 American Association for Clinical Chemistry, Inc.


Technical Briefs

Different Behaviors of Serum and Urinary CrossLaps ELISA in the Assessment of Bone Resorption in Healthy Girls

Maria Luisa Traba, Jesús A. Calero, Cioly Méndez-Dávila, Carmen García-Moreno and Concepción de la Piedraa

a address correspondence to this author at: Fundación Jiménez Díaz, Laboratorio de Bioquímica, Sección Metabolismo Mineral y Óseo, Avda Reyes Católicos 2, 28040 Madrid, Spain

Many fragments derived from collagen I degradation come to serum during bone resorption. The characterization of these fragments and the development of assays that can measure them are the basis of most of the biochemical markers of bone resorption. One of these fragments consists of two cross-linked amino acid sequences derived from the C-terminal telopeptide region of type I collagen {alpha}1 chains. Fragments containing the sequence EKAH-DGGR (CTX), with a DG site being either nonisomerized ({alpha}-CTX) or ß-isomerized (ß-CTX) were identified. Pyridinoline, deoxypyridinoline, and other cross-links linked both telopeptides (Fig. 1 ) (1). Recent reports have suggested that the proportions of nonisomerized and ß-isomerized fragments depend on bone age (1).



View larger version (12K):
[in this window]
[in a new window]
 
Figure 1. Heterogeneity of urinary degradation products of C-terminal telopeptides derived from the {alpha}1 chain of human type I collagen.

There are two available assays that can measure the ß-isomer form of the CTX epitope: urinary CrossLapsTM ELISA (2), and Serum CrossLaps One Step ELISA (3), both from . . . [Full Text of this Article]


Acknowledgments


Footnotes


References







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by the American Association for Clinical Chemistry.