Gusev N B, Sajgó M, Friedrich P
Biochim Biophys Acta. 1980 Oct 21;625(2):304-9. doi: 10.1016/0005-2795(80)90294-9.
The troponin complex isolated from rabbit skeletal muscle was cross-linked with 1,3-difluoro-4,6-dinitrobenzene, subjected to tryptic hydrolysis, and the labelled peptides were separated. One peptide was purified to homogeneity; it proved to be peptide Gly(89)-Arg(100) of troponin C on the basis of amino acid composition and N-terminal analysis. The absorption spectrum of this peptide between 300 and 500 nm was very similar to that of 1-(S-cysteinyl)-5-(N epsilon-lysyl)-2,4-dinitrobenzene, which could only be due to cross-link formation between Lys-90 and Cys-98. This finding is interpreted in terms of the proposed tertiary structure of troponin C.
从兔骨骼肌中分离出的肌钙蛋白复合物与1,3 - 二氟 - 4,6 - 二硝基苯交联，进行胰蛋白酶水解，然后分离出标记的肽段。其中一个肽段被纯化至同质；根据氨基酸组成和N端分析，它被证明是肌钙蛋白C的肽段Gly(89)-Arg(100)。该肽段在300至500纳米之间的吸收光谱与1-(S - 半胱氨酰基)-5-(Nε - 赖氨酰基)-2,4 - 二硝基苯的吸收光谱非常相似，这只能归因于Lys - 90和Cys - 98之间形成了交联。这一发现根据所提出的肌钙蛋白C的三级结构进行了解释。
