Amino acid sequence of bovine cardiac troponin I

Biochemistry ◽  
1988 ◽  
Vol 27 (8) ◽  
pp. 2821-2827 ◽  
Author(s):  
John Leszyk ◽  
Ranjana Dumaswala ◽  
James D. Potter ◽  
John H. Collins
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I

scholarly journals Human cardiac troponin I: precise identification of antigenic epitopes and prediction of secondary structure

1998 ◽  
Vol 44 (3) ◽  
pp. 487-493 ◽  
Author(s):  
Gaelle Ferrieres ◽  
Charles Calzolari ◽  
Jean-Claude Mani ◽  
Daniel Laune ◽  
Sylvie Trinquier ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Peptide Epitope ◽  
Antigenic Properties

Abstract The presence of human cardiac troponin I (hcTnI) in serum is considered to be a highly specific biochemical marker of acute myocardial infarction. To better understand the antigenic properties of hcTnI, a set of 68 overlapping peptides covering the complete amino acid sequence of hcTnI was prepared and used in epitope mapping experiments. All 16 anti-hcTnI monoclonal antibodies tested were found to recognize a peptide epitope, indicating that recognition by anti-hcTnI monoclonal antibodies was not dependent on the tertiary structure of the protein. Furthermore, the peptide reactivity with anti-hcTnI polyclonal antibodies indicated that most of the sequence of the protein was antigenic; in particular, the N- and C-terminal extremities were found to be the strongest antigenic regions. By using accurate secondary structure prediction methods, hcTnI was found to be an all-alpha type protein, with five regions predicted as helices. Matching the results of the epitope analysis with the structural prediction led us to the view that hcTnI is not a globular protein but probably adopts an extended conformation, allowing a large part of the amino acid sequence of this molecule to be recognized by the immune system. This improved knowledge of the antigenic and structural properties of hcTnI may help in developing new antibodies and immunoassays for use in diagnosing myocardial infarction.

scholarly journals The amino acid sequence of rabbit cardiac troponin I

1976 ◽  
Vol 159 (3) ◽  
pp. 633-641 ◽  
Author(s):  
R J A. Grand ◽  
J M Wilkinson ◽  
L E More
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Inhibitory Activity ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Muscle Protein ◽  
Cardiac Troponin I ◽  
Skeletal Muscle Protein ◽  
Fast Skeletal Muscle

The complete amino acid sequence of troponin I from rabbit cardiac muscle was determined by the isolation of four unique CNBr fragments, together with overlapping tryptic peptides containing radioactive methionine residues. Overlap data for residues 35-36, 93-94 and 140-145 are incomplete, the sequence at these positions being based on homology with the sequence of the fast-skeletal-muscle protein. Cardiac troponin I is a single polypeptide chain of 206 residues with mol.wt. 23550 and an extinction coefficient, E 1%,1cm/280, of 4.37. The protein has a net positive charge of 14 and is thus somewhat more basic than troponin I from fast-skeletal muscle. Comparison of the sequences of troponin I from cardiac and fast skeletal muscle show that the cardiac protein has 26 extra residues at the N-terminus which account for the larger size of the protein. In the remainder of sequence there is a considerable degree of homology, this being greater in the C-terminal two-thirds of the molecule. The region in the cardiac protein corresponding to the peptide with inhibitory activity from the fast-skeletal-muscle protein is very similar and it seems unlikely that this is the cause of the difference in inhibitory activity between the two proteins. The region responsible for binding troponin C, however, possesses a lower degree of homology. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50072 (20 pages), at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1976) 153, 5.

scholarly journals Cloning and Sequencing of Equine Cardiac Troponin I and Confirmation of Its Usefulness as a Target Analyte for Commercial Troponin I Analyzers

2005 ◽  
Vol 17 (6) ◽  
pp. 582-584 ◽  
Author(s):  
Mark Rishniw ◽  
Kenny W. Simpson
Keyword(s):  
Amino Acid ◽  
Cardiac Troponin ◽  
Myocardial Injury ◽  
Troponin I ◽  
Domestic Animals ◽  
Cardiac Troponin I ◽  
Terminal Deletion ◽  
Cloning And Sequencing ◽  
Epitope Region ◽  
Target Analyte

The analysis of cardiac troponin I (cTnI) in the diagnosis of myocardial injury in domestic animals is gaining popularity. In this study, equine cTnI was sequenced and compared with previously characterized cTnI from other species. A 6-amino-acid N-terminal deletion unique to the horse was identified. This deletion was outside the epitope region of cTnI recognized by most commercial immunoassays and did not affect the ability of a commercial analyzer system to detect recombinant equine cTnI. No function could be ascribed to the deleted portion. These data support the use of commercial analyzers in measuring equine cTnI.

scholarly journals Spiegelmer-Based Sandwich Assay for Cardiac Troponin I Detection

2020 ◽  
Vol 21 (14) ◽  
pp. 4963 ◽  
Author(s):  
Zoltán János Tolnai ◽  
Judit András ◽  
Zsuzsanna Szeitner ◽  
Krisztina Percze ◽  
László Ferenc Simon ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Sandwich Assay ◽  
Surface Plasmon Resonance Analysis ◽  
Coronary Syndrome ◽  
Resonance Analysis ◽  
Sandwich Type ◽  
Amino Acid Stretch

Two subunits of the ternary troponin complex, I and C, have cardiac muscle specific isoforms, and hence could be applied as highly-selective markers of acute coronary syndrome. We aimed at paving the way for the development of a robust cardiac troponin I-detecting sandwich assay by replacing antibodies with nuclease resistant aptamer analogues, so-called spiegelmers. To complement the previously generated spiegelmers that were specific for the N-terminus of cTnI, spiegelmers were selected for an amino acid stretch in the proximity of the C-terminal part of the protein by using a D-amino acid composed peptide. Following the selection, the oligonucleotides were screened by filter binding assay, and surface plasmon resonance analysis of the most auspicious candidates demonstrated that this approach could provide spiegelmers with subnanomolar dissociation constant. To demonstrate if the selected spiegelmers are functional and suitable for cTnI detection in a sandwich type arrangement, AlphaLisa technology was leveraged and the obtained results demonstrated that spiegelmers with different epitope selectivity are suitable for specific detection of cTnI protein even in human plasma containing samples. These results suggest that spiegelmers could be considered in the development of the next generation cTnI monitoring assays.

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