Interactions among chymotryptic troponin T subfragments, tropomyosin, troponin I and troponin C.
The 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. When a ... mixture of troponin T2 and troponin C was applied to a tropomyosin-Sepharose 4B column, neither troponin T2 nor troponin C was retained in the presence of Ca2+ ion, while only troponin T2 was bound in the absence of Ca2+ ion. Such a Ca2+-dependent effect was not observed with troponin T. Troponin T2 subfragments, except troponin T2 beta III, were retained by troponin C-Sepharose 4B in the presence of troponin I, even in the solution containing 1.0 M NaCl, in the presence and absence of Ca2+ ion. On the basis of these findings, the interactions among troponin components and tropomyosin are discussed.
Mesh Terms:
Animals, Chromatography, Affinity, Chymotrypsin, Muscles, Peptide Fragments, Rabbits, Tropomyosin, Troponin, Troponin C, Troponin I, Troponin T
Animals, Chromatography, Affinity, Chymotrypsin, Muscles, Peptide Fragments, Rabbits, Tropomyosin, Troponin, Troponin C, Troponin I, Troponin T
J. Biochem.
Date: May. 01, 1984
PubMed ID: 6746613
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