作者: Mamoru Tomita , Mitsunori Takase , Hiroyuki Wakabayashi , Wayne Bellamy
DOI: 10.1007/978-1-4615-2548-6_20
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摘要: Lactoferrin was found to contain an antimicrobial sequence near its N-terminus which appears function by a mechanism distinct from iron chelation. Antimicrobial peptides representing this domain were isolated following pepsin cleavage of human lactoferrin and bovine lactoferrin. The consist mainly loop 18 amino acid residues formed disulfide bond between cysteine 20 37 lactoferrin, or 19 36 identified contains high proportion basic residues, like various other known target microbial membranes it be located on the surface folded protein allowing interaction with components cells. domain, "lactoferrin", shown have potent broad spectrum properties effect lethal causing rapid loss colony-forming capability. Such evidence points conclusion that is structural region responsible for microbicidal also suggests possibility active produced enzymatic digestion may contribute host defense against disease.