Badley R A
Biochim Biophys Acta. 1975 Feb 27;379(2):517-28. doi: 10.1016/0005-2795(75)90159-2.
Quenching of the tryptophan fluorescence of pig serum HDL3 and LDL2 lipoproteins by iodide and succinimide has been used to estimate the accessibility of the fluorophores to the solvent and, by inference, the location of the protein in the macromolecular complexes. At least 80% of the protein is thought to be located at or near the surface in both lipoproteins but its accessibility is hindered especially in LDL2. A difference in surface topography in the two lipoproteins is suggested with the protein in LDL2 more buried in lipid and further away from the charged phospholipid polar groups than in HDL3. A refined treatment of the quenching data has been developed to take account of the heterogeneity of quenching sites found in the lipoproteins.
利用碘化物和琥珀酰亚胺对猪血清高密度脂蛋白3（HDL3）和低密度脂蛋白2（LDL2）脂蛋白的色氨酸荧光进行淬灭，以估计荧光团对溶剂的可及性，并据此推断蛋白质在大分子复合物中的位置。据认为，在这两种脂蛋白中，至少80%的蛋白质位于表面或靠近表面，但其可及性受到阻碍，尤其是在LDL2中。这两种脂蛋白的表面形貌存在差异，与HDL3相比，LDL2中的蛋白质更多地埋在脂质中，且离带电荷的磷脂极性基团更远。已开发出一种对淬灭数据的精细处理方法，以考虑脂蛋白中发现的淬灭位点的异质性。
