Digestion of troponin C with trypsin in the presence and absence of Ca2+. Identification of cleavage points

Z. Grabarek , W. Drabikowski , L. Vinokurov , R.C. Lu
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引用次数: 16

Abstract

The rate of tryptic digestion of troponin C has been shown to be dependent on Ca2+ (Drabikowski et al., Biochim. Biophys. Acta 490, 216–224). We have characterized the tryptic peptides produced both in the presence and absence of Ca2+ using amino acid composition and end-group analyses. In the presence of Ca2+ trypsin cleaves TnC at Arg-8, Lys-84 and Lys-88, leading to the formation of two large peptides, one containing the two low-affinity sites (TR1C), the other, the two high-affinity Ca2+-binding sites (TR2C). In the absence of Ca2+ (1 mM EDTA), digestion proceeds much more rapidly and takes place first at Arg-100, followed by Arg-104, Arg-120, Lys-153, Arg-8 and others. The data suggest that the points of cleavage are determined by the Ca2+-dependent conformational states of TnC, particularly in the C-terminal half of the protein where the cation is known to induce secondary structure.

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在Ca2+存在和不存在的情况下,胰蛋白酶对肌钙蛋白C的消化。解理点的鉴定
肌钙蛋白C的胰蛋白酶消化率已被证明依赖于Ca2+ (Drabikowski等人,biochem)。Biophys。学报490,216-224)。我们已经表征了色氨酸肽产生在存在和不存在Ca2+使用氨基酸组成和端基分析。在Ca2+胰蛋白酶存在的情况下,在Arg-8, Lys-84和Lys-88处切割TnC,导致形成两个大肽,一个包含两个低亲和力位点(TR1C),另一个包含两个高亲和力Ca2+结合位点(TR2C)。在没有Ca2+ (1mm EDTA)的情况下,消化过程进行得更快,首先发生在Arg-100,其次是Arg-104, Arg-120, Lys-153, Arg-8和其他。数据表明,切割点是由TnC的Ca2+依赖构象状态决定的,特别是在蛋白质的c端一半,其中阳离子已知会诱导二级结构。
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