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Molecular cloning and characterization of Taiwan macaque lactoferrin
Author(s) -
Chang JuiHsien,
Chen ChaoChung,
Chao MingChieh,
Chuang YinChing,
Chang MingChung
Publication year - 2009
Publication title -
journal of medical primatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.31
H-Index - 42
eISSN - 1600-0684
pISSN - 0047-2565
DOI - 10.1111/j.1600-0684.2008.00318.x
Subject(s) - lactoferrin , cloning (programming) , macaque , rhesus macaque , molecular cloning , biology , computational biology , genetics , gene , computer science , neuroscience , peptide sequence , programming language
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). Results and 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.