Results 381 to 390 of about 12,260,572 (400)
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The mobility of troponin C and troponin I in muscle
Journal of Molecular Recognition, 1997In vertebrate skeletal muscle, contraction is initiated by the elevation of the intracellular Ca2+ concentration. The binding of Ca2+ to TnC induces a series of conformational changes which ultimately release the inhibition of the actomyosin ATPase activity by Tnl.
Kálmán Hideg +2 more
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The Journal of Emergency Medicine, 2002
Cardiac troponins I and T are proteins integral to the function of cardiac muscle. They are very sensitive markers for the detection of myocardial damage, and the ability to assay their serum levels accurately and quickly have revolutionized the concepts of minor myocardial injury and infarction.
John, Sarko, Charles V, Pollack
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Cardiac troponins I and T are proteins integral to the function of cardiac muscle. They are very sensitive markers for the detection of myocardial damage, and the ability to assay their serum levels accurately and quickly have revolutionized the concepts of minor myocardial injury and infarction.
John, Sarko, Charles V, Pollack
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The Journal of Biochemistry, 1968
1. A method for isolation of troponin from native tropomyosin was described. 2. Troponin in combination with tropomyosin restored the whole activity of native tropomyosin in sensitizing the interaction of myosin and actin to Ca ion. 3. Troponin was found to bind nearly 4 moles of Ca per 10 5 g, of which most were exchangeable.
Fumiko Ebashi +2 more
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1. A method for isolation of troponin from native tropomyosin was described. 2. Troponin in combination with tropomyosin restored the whole activity of native tropomyosin in sensitizing the interaction of myosin and actin to Ca ion. 3. Troponin was found to bind nearly 4 moles of Ca per 10 5 g, of which most were exchangeable.
Fumiko Ebashi +2 more
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Interactions among Chymotryptic Troponin T Subfragments, Tropomyosin, Troponin I and Troponin C1
The Journal of Biochemistry, 1984The binding of various combinations of chymotryptic troponin T subfragments, troponin I and troponin C to tropomyosin, troponin C and troponin I was examined semiquantitatively by using affinity chromatography. The interaction between troponin T2 and troponin I intensified the interaction between troponin T2 (or troponin T) and tropomyosin.
Iwao Ohtsuki, Masaru Tanokura
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The binding sites of rabbit skeletal troponin-I on troponin-T
Canadian Journal of Biochemistry, 1980Various fragments derived from rabbit skeletal muscle troponin-T (Tn-T) by chemical and (or) proteolytic cleavage were mixed with whole troponin-I (Tn-I) and applied to a Sephadex G-75 gel filtration column in order to determine the binding site of Tn-I on Tn-T. This site of interaction was found to span two distinct regions of Tn-T.
Joyce R. Pearlstone, Lawrence B. Smillie
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Defining the Region of Troponin-I that Binds to Troponin-C
Biochemistry, 1999The kinetics and energetics of the binding of three troponin-I peptides, corresponding to regions 96-131 (TnI96-131), 96-139 (TnI96-139), and 96-148 (TnI96-148), to skeletal chicken troponin-C were investigated using multinuclear, multidimensional NMR spectroscopy.
Ryan T. McKay +4 more
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The Twilight Zone of Troponins
Heart Lung <html_ent glyph="@amp;" ascii="&"/> Circulation, 2003Since its introduction into the clinical environment in the early nineties, the cardiac enzyme troponin has significantly changed the way we diagnose and manage acute coronary syndromes. Troponin I is a biochemical marker of myocardial injury with a high level of specificity and sensitivity.
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An electrochemical troponin T aptasensor based on the use of a macroporous gold nanostructure
Microchimica Acta, 2019M. Negahdary +2 more
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Troponins in children and neonates
Acta Paediatrica, 2003Cardiac troponin T and cardiac troponin I—the biochemical markers of myocardial injury—are characterized by high specificity and sensitivity in comparison with other markers used in the past. Conclusion: Troponins have been studied in a wide range of clinical settings.
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