Characterization of apolipoprotein B from human serum low density lipoprotein in n-dodecyl octaethyleneglycol monoether: an electron microscope study.
We have studied the structure of the totally  delipidated polypeptide (apolipoprotein B [apo B]) present in low-density serum lipoprotein in detergent (n-dodecyl octaethyleneglycol monoether) solution by electron microscopy. The protein-detergent complex appears as a rod-shaped particle, 75-80 nm long and 4.5-5.5 nm wide. The volume of this particle is consistent with the previously published composition reported by Watt and Reynolds (1980, Biochemistry 19:1593-1598) of two copies of apo B and five to six equivalent micelles of detergent. The asymmetric particle possesses a high degree of flexibility and a strong tendency to self-associate in an orderly fashion. The extent of this association is pH dependent.
D001053:Apolipoproteins; D001055:Apolipoproteins B; D055598:Chemical Phenomena; D002621:Chemistry; D003902:Detergents; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008077:Lipoproteins, LDL / Q000032:analysis*; D008854:Microscopy, Electron; D011092:Polyethylene Glycols; D011487:Protein Conformation
D001053:Apolipoproteins; D001055:Apolipoproteins B; D003902:Detergents; D008077:Lipoproteins, LDL; C017272:dodecyloctaethyleneglycol monoether; D011092:Polyethylene Glycols