title: Purification and characterization of a glycopeptide derived from Phaseolus vulgaris leukoagglutinating phytohemagglutinin.
abstract: A glycopeptide obtained from tryptic digestion of citraconylated leukoagglutinating (L-subunit) phytohemagglutinin was isolated and purified. The composition of its ten amino acid and seven hexose residues, when compared to a previous analysis of the NH2-terminal amino acid sequence, indicated that the glycopeptide was derived from residues 11 through 20, with the oligosaccharide unit linked N-glycosidically to asparagine at the twelfth position. Structural studies involving a combination of alpha-mannosidase digestion, periodate oxidation, and permethylation, in conjunction with computerized mass-spectrometric and masschromatographic techniques, suggested a branched sequence of five mannose and two glucosamine residues similar to that found in many mammalian glycoproteins.
mesh_terms: D055598:Chemical Phenomena; D002621:Chemistry; D006020:Glycopeptides / Q000302:isolation & purification*; D009844:Oligosaccharides / Q000032:analysis; D010835:Phytohemagglutinins / Q000032:analysis*
chemical_list: D006020:Glycopeptides; D009844:Oligosaccharides; D010835:Phytohemagglutinins