McCubbin W D, Oikawa K, Kay C M
FEBS Lett. 1986 Jan 20;195(1-2):17-22. doi: 10.1016/0014-5793(86)80121-1.
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 Ca2+ binding and conformational response to Ca2+ 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 Ca2+/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 Ca2+.
已在氨基酸组成和片段化模式方面将来自火鸡骨骼肌的肌钙蛋白C与其鸡源对应物进行了比较，并通过CD和荧光监测的Ca2+结合以及对Ca2+的构象响应，将其与兔TN-C进行了比较。鸡和火鸡TN-C的溴化氰和胰蛋白酶消化混合物已通过反相HPLC进行分离。洗脱图谱的相似性以及几乎相同的氨基酸组成数据表明，序列基本相同。在pH 5.3时，火鸡和兔TN-C均结合2 mol Ca2+/mol蛋白质，而在pH 6.8时，该数字升至4 mol/mol蛋白质。圆二色性和荧光测量表明，两种蛋白质的构象对Ca2+的存在以非常相似的方式做出响应。
