
Rabbit cardiac tropomyosin was hybridized with its nonpolymerizable form, produced by treatment with carboxypeptidase A, and with a naturally occurring nonpolymerizable tropomyosin from horse platelets. Hybridization was achieved by heating equimolar mixtures to 60 degrees C in the presence of 10 mM dithiothreitol, followed by recooling. Samples of intact and carboxypeptidase-truncated tropomyosins treated in this way show lower viscosities at low ionic strength than predicted assuming random reformation of the coiled coils, suggesting that hybrids formed with one intact COOH-terminus are unable to polymerize normally. Hybridization of cardiac and platelet tropomyosins was detected by observation of the fluorescence of pyrene groups attached to cysteine residues on platelet tropomyosin.
Blood Platelets, Hot Temperature, Carboxypeptidases A, Macromolecular Substances, Protein Conformation, Viscosity, Myocardium, Carboxypeptidases, Tropomyosin, Dithiothreitol, Spectrometry, Fluorescence, Animals, Horses, Rabbits
Blood Platelets, Hot Temperature, Carboxypeptidases A, Macromolecular Substances, Protein Conformation, Viscosity, Myocardium, Carboxypeptidases, Tropomyosin, Dithiothreitol, Spectrometry, Fluorescence, Animals, Horses, Rabbits
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