Fractionation and Partial Characterization of Proteins of the Bileaflet Nuclear Membrane from Rat Liver

摘要: Abstract The sodium dodecyl sulfate (SDS)-solubilized proteins of the bileaflet nuclear membrane from rat liver have been fractionated by gel filtration. More than 23 different molecular weight classes ranging 160,000 to 16,000 can be distinguished conventional SDS-polyacrylamide electrophoresis. Polypeptide chains less were not detected. A triplet, respective which weights 64,000, 70,000, and 74,000, account for 25% total protein, while a second group in range 53,000 60,000 represents an additional 21%. amino acid composition individual fractions does exhibit large deviations delipidated membrane. trend was noted, however, progressing high low polypeptides; ratio acidic basic residues decreased 1.83 (Fraction A) 0.92 P). major portion phosphorus separated into two discrete Ten per cent eluted near void volume predominantly RNA phosphorus, whereas 80% with apparent 15,000 entirely phospholipid phosphorus. bulk neutral lipids also found this fraction; small amounts localized other column fractions. In comparing elution profiles microsomal membranes, did yield component. possibility that may represent some unique feature membrane, such as pore complex, is suggested.