Lattoferrina 200 Immuno 30 Stick Pack PromoPharma

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Lactoferrin is an 80-kDa, iron-binding glycoprotein present in milk and, to a lesser extent, in exocrine fluids such as bile and tears. It consists of a single-chain polypeptide with two gobular lobes and is relatively resistant to proteolysis. The complete cDNAs for lactoferrin from human milk, neutrophils, and bovine milk have been reported, and recombinant proteins have been produced. Owing to its iron-binding properties, lactoferrin has been proposed to play a role in iron uptake by the intestinal mucosa and to act as a bacteriostatic agent by withholding iron from iron-requiring bacteria. Its presence in neutrophils and its release during inflammation suggest that lactoferrin is also involved in phagocytic killing and immune responses. Additionally, lactoferrin may function in ways not related to iron-binding, e.g. as a growth factor and as a bactericidal agent. This review attempts to evaluate these proposed functions and their biological significance in more detail. Bellamy W, Takase M, Wakabayashi H, et al. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol 1992;73:472-9. View abstract.

Kuwata H, Yip TT, Yip CL, Tomita M, Hutchens TW (April 1998). "Bactericidal domain of lactoferrin: detection, quantitation, and characterization of lactoferricin in serum by SELDI affinity mass spectrometry". Biochemical and Biophysical Research Communications. 245 (3): 764–73. doi: 10.1006/bbrc.1998.8466. PMID 9588189. Oda H, Wakabayashi H, Tanaka M, et al. Effects of lactoferrin on infectious diseases in Japanese summer: A randomized, double-blinded, placebo-controlled trial. J Microbiol Immunol Infect. 2020 Feb 26:S1684-1182(20)30038-4. View abstract. GRAS Notice No. GRN 000130. 2003. Available at: https://www.cfsan.fda.gov/~rdb/opa-g130.html (Accessed 29 June 2005). Pursel VG (1998). "Modification of Production Traits". In Clark AJ (ed.). Animal Breeding: Technology for the 21st Century (Modern Genetics). Boca Raton: CRC. p.191. ISBN 978-90-5702-292-0. Drobni P, Naslund J, Evander M. Lactoferrin inhibits human papillomavirus binding and uptake in vitro. Antiviral Res 2004;64:63-8. View abstract.

van't Land B, van Beek NM, van den Berg JJ, M'Rabet L. Lactoferrin reduces methotrexate-induced small intestinal damage, possibly through inhibition of GLP-2-mediated epithelial cell proliferation. Dig Dis Sci 2004;49:425-33. . View abstract. Lactoferrin belongs to the basic proteins, its isoelectric point is 8.7. It exists in two forms: iron-rich hololactoferrin and iron-free apolactoferrin. Their tertiary structures are different; apolactoferrin is characterized by "open" conformation of the N-lobe and the "closed" conformation of the C-lobe, and both lobes are closed in the hololactoferrin. [22]

a b Giansanti F, Rossi P, Massucci MT, Botti D, Antonini G, Valenti P, Seganti L (2002). "Antiviral activity of ovotransferrin discloses an evolutionary strategy for the defensive activities of lactoferrin". Biochemistry and Cell Biology. 80 (1): 125–130. doi: 10.1139/o01-208. PMID 11908636. Abbondantissima nel colostro umano o primo latte, la lattoferrina circola nell'organismo prevalentemente nel plasma sanguigno. Zhang GH, Mann DM, Tsai CM. Neutralization of endotoxin in vitro and in vivo by a human lactoferrin-derived peptide. Infect Immun 1999;67:1353-8. View abstract.Vorland LH, Ulvatne H, Andersen J, et al. Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin. Scand J Infect Dis 1998;30:513-7. View abstract.