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- W2048383876 abstract "The delipidated protein moiety, apolipoprotein B, of human low-density lipoproteins was permethylated in potassium butoxide/dimethyl sulfoxide with methyl iodide. The derivatized protein was soluble in dimethyl sulfoxide and, in the presence of sodium dodecyl sulfate, in an aqueous buffer. Analysis of the methylated apolipoprotein B by polyacrylamide gradient gel electrophoresis in the presence of sodium dodecyl sulfate revealed five discrete bands of lower molecular mass than that of the parent 265-kDa protein, which disappeared upon permethylation. The electrophoretic behavior of the methylated apolipoprotein B was distinctly different from that of the other methylated proteins studied, including transferrin, bovine serum albumin, aldolase, beta-lactoglobulin, and apolipoprotein A-I, all of which had a higher apparent molecular weight after permethylation as compared to the corresponding native polypeptide. Calculated on the basis of methylated standard proteins the five polypeptides of apolipoprotein B have apparent molecular masses of 9.0, 16.6, 25.6, 35.7, and 46.7 kDa. The results suggest that the protein moiety of human low-density lipoprotein consists of subunits. In general, the results indicate that the permethylation method can be used to solubilize hydrophobic proteins in organic solvents for structural studies." @default.
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- W2048383876 date "1985-08-01" @default.
- W2048383876 modified "2023-09-27" @default.
- W2048383876 title "Solubilization of proteins in dimethyl sulfoxide by permethylation: Application to structural studies of apolipoprotein B" @default.
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- W2048383876 doi "https://doi.org/10.1016/0003-2697(85)90240-4" @default.
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