Physical and chemical characterization of the major outer membrane protein of Rhodopseudomonas sphaeroides.
The characterization of the major outer membrane protein of Rhodopseudomonas sphaeroides is described. Molecular weight estimations using Ferguson plots derived from sodium dodecyl sulfate and urea-polyacrylamide gels were 39,500 and 32,200, respectively, in good agreement with the value of 33,800 obtained from amino acid compositional studies. NH2-terminal amino acid determinations of the major outer membrane protein revealed a blocked NH2 terminus. Gas chromatography of the acid-hydrolyzed protein confirmed the presence of fatty acid covalently associated with the protein presumably through an amino linkage. Peptide mapping of tryptic and chymotryptic digestions of the protein led to the identification of one peptide in each digest containing fatty acid. Digestion of the fatty acid-containing peptide with pronase resulted in the fatty acid together with L-alanine becoming extractable into hexane. We conclude that the major outer membrane protein of R. sphaeroides is a proteolipid containing at least 1 mol of fatty acid/mol of protein in amide linkage to the NH2-terminal L-alanine of the protein.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin; D005227:Fatty Acids / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011402:Pronase; D012242:Rhodobacter sphaeroides / Q000032:analysis*; D014357:Trypsin
D000596:Amino Acids; D001426:Bacterial Proteins; D005227:Fatty Acids; D008565:Membrane Proteins; D010446:Peptide Fragments; D002918:Chymotrypsin; D014357:Trypsin; D011402:Pronase