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  • Title: Purification and characterization of minor brain proteolipids: use of fast atom bombardment-mass spectrometry for peptide sequencing.
    Author: Lepage P, Helynck G, Chu JY, Luu B, Sorokine O, Trifilieff E, Van Dorsselaer A.
    Journal: Biochimie; 1986 May; 68(5):669-86. PubMed ID: 3089328.
    Abstract:
    A combination of lipophilic gel permeation chromatography and ion-exchange chromatography in organic solvents was used to purify low molecular weight proteolipids from bovine brain. Cleavage peptides were purified by HPLC and studied mainly by the fast atom bombardment--mass spectrometry technique. A proteolipid of Mr 14 000 contains several peptides from the first 113 amino acids of the major myelin proteolipid (MMPL) plus an extra unknown blocked N-terminal peptide. A proteolipid of Mr 16 000 contains smaller peptides belonging to a C-terminal fragment of MMPL of about 160 residues. These two proteolipids do not seem to be artifacts from MMPL.
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