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Comparative calcium binding and conformational studies of turkey and rabbit skeletal troponin C
Author(s) -
McCubbin William D.,
Oikawa Kimio,
Kay Cyril M.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80121-1
Subject(s) - chemistry , troponin c , cyanogen bromide , circular dichroism , mole , fluorescence , troponin t , amino acid , calcium , biochemistry , chromatography , stereochemistry , troponin , peptide sequence , organic chemistry , psychology , physics , quantum mechanics , psychiatry , myocardial infarction , gene
Troponin C from turkey skeletal muscle has been compared with its chicken counterpart in terms of amino acid composition and fragmentation patterns and with rabbit TN‐C by Ca 2+ binding and conformational response to Ca 2+ as monitored by CD and fluorescence. Cyanogen bromide and tryptic digestion mixtures of chicken and turkey TN‐C have been separated by reversed‐phase HPLC. The similarity of the elution profiles, along with the almost identical amino acid compositional data, suggest that the sequences are essentially equivalent. Both turkey and rabbit TN‐C bound 2 mol Ca 2+ /mol protein at pH 5.3, while at pH 6.8, this figure was raised to 4 mol/mol protein. Circular dichroism and fluorescence measurements indicated that the conformations of the two proteins responded in a very similar manner to the presence of Ca 2+