Pellicone C, Bouillon P, Virmaux N, Vincendon G
Biochimie. 1981 Aug-Sep;63(8-9):671-6. doi: 10.1016/s0300-9084(81)80215-5.
The 50 amino acid residues sequence of a hydrophobic region of bovine rhodopsin, a membrane protein of retinal rod photoreceptors of molecular weight 39,000 was determined. This primary structure determination was performed on the S5 fragment (about 12,000 molecular weight) obtained from 2-(2 nitrophenylsulfenyl)-3-methyl-3'bromo-indolenine cleavage of the protein. Automatic Edman degradation used in liquid phase was performed in presence of N-cetyl-N,N,N-trimethyl-ammoniumbromide, a cationic detergent incorporated in the proteic film. S5 is a C-terminal rhodopsin fragment and contains the phosphorylation sites. The covalent structure determined overlaps with the sequence of an already known fragment [1]; thus 25 per cent of the rhodopsin primary structure is now elucidated. Our results are in agreement with and chiefly refine the topological model for rhodopsin which correlates its membrane location and its functional sites.
测定了牛视紫红质（一种分子量为39,000的视网膜视杆光感受器的膜蛋白）疏水区域的50个氨基酸残基序列。该一级结构测定是在通过2-(2-硝基苯磺酰基)-3-甲基-3'-溴吲哚宁裂解该蛋白获得的S5片段（分子量约12,000）上进行的。在蛋白质膜中掺入的阳离子去污剂N-十六烷基-N,N,N-三甲基溴化铵存在下，进行了液相自动埃德曼降解。S5是视紫红质的C末端片段，包含磷酸化位点。所确定的共价结构与一个已知片段的序列重叠[1]；因此，视紫红质一级结构的25%现已阐明。我们的结果与视紫红质的拓扑模型一致，并且主要对其进行了完善，该模型将其膜定位与其功能位点联系起来。
