Hydrodynamic properties of bovine cardiac troponin-I and troponin-T.
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Hydrodynamic properties of bovine cardiac troponin-I and troponin-T.
Bovine cardiac troponin-I (TN-I) and troponin-T (TN-T) have been examined in solution using ultracentrifugation, gel filtration, and viscosity. A new method of purifying TN-T, employing hydroxylapatite chromatography in 6 M urea, is reported. Cardiac TN-T (Mr = 36,000) undergoes a reversible, concentration-dependent association in nondenaturing buffers, probably to a tetramer. The Stokes radius...
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We have investigated the structure of the cTnC-cTnI-cTnT(198-298) calcium-saturated, ternary cardiac troponin complex by small-angle scattering with contrast variation. Shape restoration was also applied to the scattering information resulting from the deuterated cTnC subunit, the unlabeled cTnI-cTnT(198-298) subunits, and the entire complex. The experimental results and modeling indicate that ...
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We report on the isolation of two bovine cardiac troponin isoforms which differ in sequence near the amino terminus of troponin T (Risnik, V. V., Verin, A. D., and Gusev, N. B. (1985) Biochem. J. 225, 549-552). The isoforms were isolated by direct separation on DEAE-cellulose and were also obtained by reconstitution of urea-dissociated subunits. The two isoforms were compared for their effects ...
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The effect troponin I phosphorylation has on the Ca2+-binding properties of troponin C (TnC) in the whole troponin complex reconstituted from cardiac troponin I (TnI), troponin T, and TnC has been measured. To selectively follow Ca2+ binding at the Ca2+-specific sites of TnC, this subunit was labeled with the fluorescent probe 2-(4’-iodo-acetamidoanilino)naphthalene-6sulfonic acid before recons...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)32812-6