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• W1867363027 abstract "1. Eight peptides were separated from the CNBr digest of troponin T from rabbit white skeletal muscle and characterized. 2. By study of the amino acid sequence of the methionine-containing peptides isolated after chymotryptic and tryptic digestion and of the N- and C-terminals of the CNBr peptides, six of the latter were shown to be arranged in the sequence CNB1-CNB2-CNB5-CNB6-CNB8-CNB7. The other two peptides, CNB1' and CNB3, have been shown to be partial digestion products. 3. The CNBr peptides CNB1' and CNB2 contained a common sequence and were the only peptides in CNBr digests of troponin T that formed a complex with tropomyosin as judged by viscometric and electrophoretic studies. 4. It is concluded that tropomyosin interacts with the N-terminal half of the troponin T molecule approximately in the region lying between residues 70 and 160. 5. Electrophoretic evidence indicates that tropomyosin and troponin C interact with troponin T. 6. None of the major CNBr peptides of troponin T isolated formed a complex with troponin C on electrophoresis at pH 8.6." @default.
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• W1867363027 date "1975-10-01" @default.
• W1867363027 modified "2023-10-14" @default.
• W1867363027 title "The primary structure of troponin T and the interaction with tropomyosin" @default.
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• W1867363027 doi "https://doi.org/10.1042/bj1510085" @default.
• W1867363027 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1172328" @default.
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