Ruggiero A C, Meirelles N C
Departamento de Bioquímica, Instituto de Biologia, Campinas, SP, 13801, Brasil.
Mol Genet Metab. 1998 Jun;64(2):148-51. doi: 10.1006/mgme.1998.2689.
The chemical modifications induced by trifluoperazine (TFP) in erythrocyte ghosts have been investigated by fluorescence quenching. The apparent distance separating the membrane protein tryptophans and bound 1-aniline-8-naphthalene sulfonate (ANS) molecules decreased after treating erythrocyte membranes with TFP. This effect was accompanied by a significant decrease in the maximum efficiency of energy transfer. We conclude that TFP-induced alterations in the structure of membrane proteins lead to a rearrangement of the surrounding lipids, and consequently to local conformational changes in membrane organization.
通过荧光猝灭研究了三氟拉嗪（TFP）对红细胞血影的化学修饰作用。用TFP处理红细胞膜后，膜蛋白色氨酸与结合的1-苯胺-8-萘磺酸盐（ANS）分子之间的表观距离减小。这种效应伴随着能量转移最大效率的显著降低。我们得出结论，TFP诱导的膜蛋白结构改变导致周围脂质重排，进而导致膜组织局部构象变化。
