Lactoferrin: Interactions and Biological Functions by Jeremy H. Brock (auth.), T. William Hutchens, Bo Lönnerdal

By Jeremy H. Brock (auth.), T. William Hutchens, Bo Lönnerdal (eds.)

In Lactoferrin: Interactions and organic capabilities, experimental and scientific investigators sign up for forces to provide an explanation for our present realizing of lactoferrin, a hugely major protein in medication and undefined. Drawing on many disciplines, the front-line professionals writing right here outline the structural beneficial properties of lactoferrin and describe intimately numerous of its physiological features. those comprise the position of lactoferrin in killing micro organism, and its involvement in mobilephone development and proliferation, within the modulation of immune functionality, and in iron absorption. specific cognizance is given to lactoferrin capabilities within the law of standard and diseased states. New wisdom of the molecular biology of lactoferrin can also be integrated, besides discussions of commercially attainable large-scale construction options and demanding new commercial purposes.

Lactoferrin: Interactions and organic features bargains a complete, multidisciplinary view of our current wisdom of lactoferrin and opens tips to the drastically elevated use of lactoferrin as a bioactive reagent in meals and prescription drugs. Now the hot typical reference within the box, Lactoferrin will end up necessary to all these operating with this crucial biochemical in either easy and medical settings.

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223-244. , Fortuna, M. , Swamy, C. V. , and Das, M. R. (1989) Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity. f. Exp. Med. 170,415-429. , and Ravazzolo, R. (1992) Lactoferrin binding sites and nuclear localization in K562(S) cells. f. Cell Physiol. 153,477-482. Griffiths, E. and Bullen, J. J. (1987) Iron binding proteins and host defence, in Iron and Infection (Bullen, J. J. ), Wiley, Chichester, UK, pp.

Anderson, B. , Baker, H. , Norris, G. , Rumball, S. , and Baker, E. N. (1990) Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins. ) 344, 784-787. Baker, E. , Baker, H. , Smith, C. , Stebbins, M. , Hellstrom, K. , and Hellstrom, I. (1992) Human melanotransferrin (p97) has only one functional iron-binding site. FEBS Lett. 298,215-219. Baker, E. N. (1994) Structure and reactivity of transferrins. Adv. Inorg. Chern. 41, 389-463. Baker, H. , Day, C. , Norris, G.

1993), since the D60S mutant is still able to close. Rather, it is part of the "lock" that holds the domains closed; the main part of the "lock" is provided by the iron atom itself, and loss of Asp 60 weakens but does not prevent domain closure. Its importance appears also to be as a "prop" that defines the extent of closure; in its absence the domains collapse inward by 7°. If a correctly closed structure is required for receptor binding, as is believed to be the case for the related periplasmic binding proteins, Asp 60 thus may be of critical importance.

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