Sutton D A, Drewes S E, Welz U
Biochem J. 1972 Nov;130(2):589-95. doi: 10.1042/bj1300589.
The new protein reagent 1-fluoro-2-nitro-4-trimethylammoniobenzene iodide reacts with model amino acids to give derivatives that are very stable to hydrolysis. In a dimethyl sulphoxide-water medium it reacts rapidly (3h) with bovine insulin, and substitution occurs quantitatively at the N-terminal amino groups and at the in-amino groups of lysine residues. Two of the four tyrosine residues react, and it is assumed that these are the exposed groups leaving the buried groups unattacked. Unlike 1-fluoro-2,4-dinitrobenzene and related reagents, it imparts hydrophilic properties to the protein derivative, thus facilitating structural and other studies on the derivative. Circular-dichroism spectra of the modified insulin suggest that no conformational changes have occurred during reaction. These spectra also reveal the presence of an extrinsic Cotton effect at 410nm.
新型蛋白质试剂1-氟-2-硝基-4-三甲基碘化铵苯与模型氨基酸反应生成对水解非常稳定的衍生物。在二甲基亚砜-水介质中，它能迅速（3小时）与牛胰岛素反应，取代反应定量地发生在N端氨基和赖氨酸残基的ε-氨基上。四个酪氨酸残基中有两个发生反应，据推测这些是暴露在外的基团，而埋藏的基团未受攻击。与1-氟-2,4-二硝基苯及相关试剂不同，它赋予蛋白质衍生物亲水性，从而便于对衍生物进行结构及其他研究。修饰胰岛素的圆二色光谱表明反应过程中未发生构象变化。这些光谱还揭示在410nm处存在非固有科顿效应。
