title: Molecular cloning and characterization of Taiwan macaque lactoferrin.
abstract: BACKGROUND
  Lactoferrin (LF) is an iron-binding glycoprotein that plays an important role in combating a wide range of pathogens and contributes innate protective defenses of mammals.
  
  
  METHODS
  We cloned and sequenced the full-length cDNA for LF from Taiwan macaque. The antimicrobial activity and iron-binding ability of the purified recombinant macaque LF (rmLF) were determined and compared with those of human LF (hLF).
  
  
  CONCLUSIONS
  The complete mLF cDNA (GenBank: EU523857) encoded a 710-aa precursor with a 19-aa signal peptide. The nucleotide sequence of mLF showed the highest identity to the rhesus monkey LF (98%), whereas the putative amino acid sequence of mLF showed the highest identity to the hLF (90%). The rmLF and natural hLF showed almost equivalent antibacterial activities against Klebsiella pneumoniae and mLF presented a slightly lower activity against Listeria monocytogenes than natural hLF. In addition, the patterns of iron release from mLF and hLF were nearly identical.
authors.affiliation: Department of Parasitology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
authors.forename: Jui-Hsien
authors.initials: JH
authors.lastname: Chang
authors.forename: Chao-Chung
authors.initials: CC
authors.lastname: Chen
authors.forename: Ming-Chieh
authors.initials: MC
authors.lastname: Chao
authors.forename: Yin-Ching
authors.initials: YC
authors.lastname: Chuang
authors.forename: Ming-Chung
authors.initials: MC
authors.lastname: Chang