The primary structure of the phosphatidylcholine-exchange protein from bovine liver. Isolation and characterization of the staphylococcal protease peptides and the amino-acid sequence of the N-terminal half (residues 1--122).
The phosphatidylcholine exchange protein from bovine liver consists of a single polypeptide chain and has a blocked N terminus. The protein contains an estimated 244 amino acid residues in accordance with a determined molecular weight of 28000. The protease from mouse submaxillaris gland cleaved the citraconylated and S-carboxymethylated derivative of the exchange protein at one specific site (Arg14-Glu15) close to the N terminus. Analysis of the two resulting peptides showed that N-acetyl-methionine was the N-terminal residue and gave the sequence of the first 41 residues. The modified protein was also fragmented with the protease from Staphylococcus aureus. The peptides isolated represented 88% of the protein; their sequences were determined by manual and automated Edman degradation. Alignment of a number of these peptides gave the complex sequence of the N-terminal half up to position 122.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000727:Androgen-Binding Protein; D000818:Animals; D002352:Carrier Proteins; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D008099:Liver / Q000032:analysis*; D051379:Mice; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D010447:Peptide Hydrolases; D049294:Phospholipid Transfer Proteins; D013211:Staphylococcus aureus / Q000201:enzymology; D013363:Submandibular Gland / Q000201:enzymology; D014357:Trypsin; D014364:Tryptophan / Q000032:analysis
D000596:Amino Acids; D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D010446:Peptide Fragments; D049294:Phospholipid Transfer Proteins; D014364:Tryptophan; D010447:Peptide Hydrolases; D014357:Trypsin