Purification and characterization of minor brain proteolipids: use of fast atom bombardment-mass spectrometry for peptide sequencing.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003488:Cyanogen Bromide; D013058:Mass Spectrometry; D008970:Molecular Weight; D010446:Peptide Fragments; D011510:Proteolipids / Q000302:isolation & purification*; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D011510:Proteolipids; D014357:Trypsin; D003488:Cyanogen Bromide