Lactoferrin Structure-Function Relationships

作者: Jeremy H. Brock

DOI: 10.1007/978-1-4612-3956-7_1

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摘要: Although lactoferrin was first isolated over 30 years ago, its function remains unclear. Structurally, it closely resembles the iron-transport protein transferrin, suggesting that may also have an role, and lactoferrin-binding sites or receptors been reported on a variety of cells tissues. However, high pI (~8.5–9.0) allows to interact with many macromolecules, which makes identification genuine difficult. The idea in breast milk acts as specific transporter iron mucosal infant gut could explain bioavailability iron, but good evidence for this is lacking, there are indications actually inhibit absorption. Another possible antimicrobial agent, particularly gut, at inflammatory foci where released by degran-ulating neutrophils. There ample vitro exerts bacteriostatic effect through ability sequester more recently, bactericidal activity independent iron-binding mediated N-terminal basic peptide has reported. disappointingly few vivo data support hypothesis. Lactoferrin various effects immune system, such regulation antibody production, complement activation, natural killer (NK) cell function, not known how carries out these activities. biological role thus enigma.

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