title: [Mannosylation of ligand binding domain 2 of HER-2/neu].
abstract: OBJECTIVE
  To establish a new method for protein mannosylation, which will facilitate the study of antigen presentation mediated by mannose receptor.
  
  
  METHODS
  Recombinant HER-2/neu ligand binding domain 2 (LBD2) was purified through DEAE sepharose FF column and cobalt-based affinity resins. LBD2 protein was mannosylated in-vitro,and then analyzed by MALDI-TOF-MS and resorcinol-sulfuric acid method.
  
  
  RESULTS
  The purity of LBD2 obtained was 90%. Analysis of MALDI-TOF-MS and resorcinol-sulfuric acid method suggested LBD2 was mannosylated.
  
  
  CONCLUSIONS
  LBD2 neoglycoprotein has been obtained, which lays the foundation for the study of antigen uptake and presentation mediated by mannose receptor and the development of tumor vaccine.
authors.affiliation: Institute of Basic Medical Sciences, Academy of Military Medical Sciences, Beijing 100850, China.
authors.forename: Ming
authors.initials: M
authors.lastname: Xu
authors.forename: Ning
authors.initials: N
authors.lastname: Guo
authors.forename: Hong-xia
authors.initials: HX
authors.lastname: Wang
authors.forename: Ai-ling
authors.initials: AL
authors.lastname: Li
authors.forename: Mei-ruo
authors.initials: MR
authors.lastname: Hu
authors.forename: Bei-fen
authors.initials: BF
authors.lastname: Shen
mesh_terms: D001665:Binding Sites; D015153:Blotting, Western; D008024:Ligands; D008358:Mannose / Q000378:metabolism*; D008970:Molecular Weight; D018719:Erb-b2 Receptor Tyrosine Kinases / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D008024:Ligands; D008358:Mannose; D018719:Erb-b2 Receptor Tyrosine Kinases; D011994:Recombinant Proteins