Advances in Lactoferrin Research by Edward N. Baker, Bryan F. Anderson, Heather M. Baker

By Edward N. Baker, Bryan F. Anderson, Heather M. Baker (auth.), Geneviève Spik, Dominique Legrand, Joël Mazurier, Annick Pierce, Jean-Paul Perraudin (eds.)

Following the 2 conferences on Lactoferrin constitution and serve as that have been held in Honolulu, Hawaii, in 1993 and 1995, the 3rd overseas convention on Lactoferrin constitution and serve as used to be held in Le Touquet, France, and has effectively bolstered and diverse the formerly created bridges among biochemists, clinicians, and firms. in reality, scientists, physicians, and other people of from various domain names have introduced a wealth of contemporary info bearing on biochemistry and technical advances within the identity of lactoferrin-derived compounds in addition to phone biology, molecular biol­ ogy, pathology, and clinical purposes of lactoferrin and lactoferrin-derived com­ kilos. We have been so overjoyed with the swift development of information relating many biologi­ cal and immunological capabilities of lactoferrins and the relationships among their struc­ ture and serve as, we would have liked to percentage our excitement with the readers drawn to this box. the current booklet. which represents a assessment of a few of the main intriguing contributions, is meant to mirror the prestige of our wisdom and transmit our hopes for the long run devel­ opment of in vivo functions of average and recombinant lactoferrins. we want to precise our gratitude to the sponsors who contributed to the or­ ganization of the assembly in this type of friendly position and allowed the participation of numerous younger researchers. we might additionally prefer to thank all of the contributors who've spoke back with enthusiasm our invitation and to each one of many Laboratoire de Chimie Biologique for the consistent and effective help.

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21, 151--159. 21. , and Tomita, M. ( 1992) Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol. 73, 472--47'1. 22. , and Fujita, K. (1983) Development and differences of intestinal tlora in the neonatal period in breast-fed and bottle-fed infants. Pediatrics 27, 317-320. 4 ANALYSIS OF BOVINE LACTOFERRIN IN WHEY USING CAPILLARY ELECTROPHORESIS (CE) AND MICELLAR ELECTROKINETIC CHROMATOGRAPHY (MEKC) Peter Riechel, 1 Torsten Wei/3, 1 Roland Ulber, 1 Heinrich Buchholz, 2 and Thomas Schepcr 1 Institut filr Technische Chemic Universitat Hannover CallinstraGe 3, 30 167 Hannover, Germany 2 BIOLAC GmbH Am Bahnhof I, 3 I 097 Harbansen, Germany 1 1.

And His 253 in N-Iobe and corresponding Tyr 435 and 528, Asp 395 and His 597 in the Clobe). The two oxygens from bidentate carbonate ion complete a distorted octahedral geometry at the metal ion. It also provides two ligands to the iron atom. The carbonate ion occupies a pocket formed by two positively charged groups of Arg side chain (Arg 121 in N-Iobe and Arg 465 inC-lobe) and N-terminus of helix 121-136, making good hydrogen bonds with both. There are few difference in anion binding site between two lobes.

9. METAL AND ANION SITE The iron binding sites are extremely similar in all the lactoferrins. ) 2 Tyr, I Asp and I His (Tyr 92 and 192, Asp 60 20 A. K. Sharma et at. and His 253 in N-Iobe and corresponding Tyr 435 and 528, Asp 395 and His 597 in the Clobe). The two oxygens from bidentate carbonate ion complete a distorted octahedral geometry at the metal ion. It also provides two ligands to the iron atom. The carbonate ion occupies a pocket formed by two positively charged groups of Arg side chain (Arg 121 in N-Iobe and Arg 465 inC-lobe) and N-terminus of helix 121-136, making good hydrogen bonds with both.

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