Sekine T, Hikita S, Muno D
J Biochem. 1984 Aug;96(2):571-3. doi: 10.1093/oxfordjournals.jbchem.a134869.
Trinitrobenzene selectively dinitrophenylates SH1, a specific thiol in the myosin heavy chain which contains 1 mol of this cysteinyl residue. When the SH1-DNP-myosin thus obtained was irradiated with a mercury lamp, a cross-linked product was formed with a molecular weight of about 220K daltons. It was shown that this product was composed of both heavy and light chains by fluorescence labeling of the heavy chain at SH2, another specific thiol, and immune reaction using an anti-light chain antibody, respectively.
三硝基苯选择性地将肌球蛋白重链中的特定硫醇SH1二硝基苯化，该肌球蛋白重链含有1摩尔这种半胱氨酰残基。当如此得到的SH1 - DNP - 肌球蛋白用汞灯照射时，形成了一种分子量约为220千道尔顿的交联产物。分别通过在另一个特定硫醇SH2处对重链进行荧光标记以及使用抗轻链抗体进行免疫反应表明，该产物由重链和轻链组成。
