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


     

Clinical Chemistry 43: 1088-1089, 1997;
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 ISI 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 ISI Web of Science (2)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lozano, D.
Right arrow Articles by Méndez, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lozano, D.
Right arrow Articles by Méndez, M.
Related Collections
Right arrow Proteomics and Protein Markers
(Clinical Chemistry. 1997;43:1088-1089.)
© 1997 American Association for Clinical Chemistry, Inc.

Technical Briefs

Analytical Performance of the Sanofi Access® Cardiac Troponin-I Procedure

Diego Lozanoa, Pino Carreño, Inmaculada Moreno and Manuel Méndez

a address for correspondence and present address: c/Ferrocarril del Puerto 16 5-C, 29002 Malaga, Spain

Troponin-I (TnI), a regulatory protein of the thin filaments of striated muscle, is part of the troponin complex (I, T, C) involved in the calcium-sensitive switch that regulates the interaction of actin and myosin in these tissues (1). TnI exists in three isoforms: one for slow-twitch, one for fast-twitch, and one for cardiac muscle. Cardiac TnI (cTnI) is differentiated from the skeletal muscle isoform by a significant difference in amino acid sequence (2). cTnI is not expressed in human fetal skeletal muscle or in adult human skeletal muscle in response to any pathological stimuli but is specific to cardiac muscle. Consequently, an increasing interest has been paid to this protein as a marker of myocardial injury (3)(4).

Several different immunoassays have been reported for quantification of cTnI in serum. They use two cTnI-specific monoclonal antibodies, do not show cross-reactivity with skeletal muscle TnI or other cardiac proteins, and are not . . . [Full Text of this Article]


Acknowledgments


Footnotes


References






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1997 by the American Association for Clinical Chemistry.