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Clinical Chemistry 50: 786-787, 2004; 10.1373/clinchem.2003.025924
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(Clinical Chemistry. 2004;50:786-787.)
© 2004 American Association for Clinical Chemistry, Inc.


Letters to the Editor

Time for Troponin T? Implications from Newly Elucidated Structure

Ravinder Sodi1,a, Simon Darn1 and Anthony Stott1

1 Department of Clinical Chemistry, Royal Liverpool and Broadgreen, University Hospitals, Prescot Street, Liverpool L7 8XP, United Kingdom

aAuthor for correspondence. Fax 44-0151-706-4250; e-mail ravsodi@yahoo.com.

The first 20% of the full text of this article appears below.


To the Editor:

The recent publication of the structure of the core domain of the troponin complex in Nature (1) has prompted us to ask: "What is the cardiac troponin T (cTnT) assay actually measuring?"

Roche Diagnostics Corporation has developed an electrochemiluminescence assay for cTnT (Roche E170), which detects free cTnT and binary/ternary troponin complexes released into the serum after a myocardial infarction (2). This assay uses two antibodies (M7 and M11.7) that recognize two specific epitopes (residues 125–131 and 136–147, respectively). The cTnT protein itself consists of 288 amino acids. From the study by Takeda et al. (1), we have been able to ascertain that the amino acid sequences of . . . [Full Text of this Article]




The following articles in journals at HighWire Press have cited this article:


Home page
Clin. Chem.Home page
M. N. Fahie-Wilson, D. J. Carmichael, M. P. Delaney, P. E. Stevens, E. M. Hall, and E. J. Lamb
Cardiac Troponin T Circulates in the Free, Intact Form in Patients with Kidney Failure
Clin. Chem., March 1, 2006; 52(3): 414 - 420.
[Abstract] [Full Text] [PDF]




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