Eremin A N, Metelitsa D I, Smettan G
Biokhimiia. 1984 Jun;49(6):976-84.
The interactions of myoglobin, cytochrome c, and cytochrome P-450 LM-2 isolated from rabbit liver microsomes with detergents of type A (TM 3-12, Tween 20, Triton N-101) and detergent of B type (sodium cholate) in aqueous media were studied. These interactions are accompanied by a decrease in the Soret band intensity for all three hemoproteins. The rate of this process depends on the nature and concentration of the detergent as well as on temperature. The rate of the Soret band decrease is maximal for the zwitter-ionic surfactant TM 3-12. The rate constants of hemoprotein transformation depend on the detergent concentration. The detergent effects on the conformation and structure of the protein were demonstrated, using CD spectra and second derivatives of the absorption spectra of the hemoproteins in the presence of the detergents. The activation energies for myoglobin transformation in the presence of various detergents are equal to 17-23 kcal/mol and possibly reflect the cleavage of the coordinative heme-apoprotein bonds. A model of detergent interaction with hemoproteins is discussed. According to this model, the bimolecular interaction of the proteins with surfactants is observed at the detergent concentrations that are much lower than those for critical micelle formation values.
研究了从兔肝微粒体中分离出的肌红蛋白、细胞色素c和细胞色素P - 450 LM - 2在水性介质中与A型洗涤剂（TM 3 - 12、吐温20、 Triton N - 101）和B型洗涤剂（胆酸钠）的相互作用。所有这三种血红素蛋白的索雷特带强度都随着这些相互作用而降低。该过程的速率取决于洗涤剂的性质和浓度以及温度。两性离子表面活性剂TM 3 - 12使索雷特带降低的速率最大。血红素蛋白转化的速率常数取决于洗涤剂浓度。利用圆二色光谱（CD光谱）和血红素蛋白在洗涤剂存在下吸收光谱的二阶导数，证明了洗涤剂对蛋白质构象和结构的影响。在各种洗涤剂存在下肌红蛋白转化的活化能等于17 - 23千卡/摩尔，这可能反映了血红素 - 载脂蛋白配位键的断裂。讨论了洗涤剂与血红素蛋白相互作用的模型。根据该模型，在远低于临界胶束形成值的洗涤剂浓度下，观察到了蛋白质与表面活性剂的双分子相互作用。
