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Lactotransferrin rabbit

Since these first discoveries, lactotransferrin has been isolated from milk of numerous mammals goat [40], mare [41], monkey [42], mouse [43,44], rabbit [45] and sow [46,47]. [Pg.206]

Structural comparison of the iron binding sites of N-lobe of rabbit serotransferrin, human lactotransferrin and... [Pg.210]

Iron transport. Experiments in vitro carried out in 1979 by Cox et al. [164] and using human intestinal biopsies demonstrated that human lactotransferrin can donate iron to intestinal mucosal cells. The characterization of a specific intestinal lactotransferrin receptor in rabbit [48], mouse [165,166], Rhesus monkey [167] and human foetal intestinal brush border membranes [168] reinforces the concept of the role of lactotransferrin in intestinal iron absorption. However, despite these findings, the nutritional activity of lactotransferrin is still a subject of controversy (for a review, see ref. [7]). [Pg.217]

Lactotransferrin receptors. The existence of a lactotransferrin receptor was first demonstrated by Van Snick and Masson in 1976 [191] at the surface of mouse peritoneal macrophages and lymphocytes. Since this discovery, the presence of lactotransferrin receptors has been demonstrated at the surface of various cells (for reviews, see refs. [156,158,192,193]) rabbit [48], mouse [165,166], monkey [167] and human [168] enterocytes human HT29 and Caco-2 enterocyte cell lines [194] human monocytes (reviewed in ref. [195]), human alveolar macrophages [196], human neutrophils [195,197], human resting lymphocytes [197], human activated lymphocytes [189], human Jurkat T cell line [190], human epithelial mammary cell line [198], human platelets [199,200] and megakaryocytes [201], hepatocytes [202,203] and in bacteria (for a review see refs. [204,205]). [Pg.218]

As mentioned above (see section 2.2.1), the three-dimensional structure of the peptide chains of rabbit serotransferrin, of human and bovine lactotransferrins and of ovotrans-... [Pg.231]

As mentioned above. X-ray diffraction of transferrin furnishes little information on the 3D-structure of the glycans and the images we have today remain largely speculative since they result from molecular modelling studies. We have represented in Fig. 21 the 3D-structure, determined by molecular modelling on the basis of X-ray diffraction data of rabbit serotransferrin [276] and of human lactotransferrin [89,92]. In rabbit serotransferrin, the single glycan linked to the peptide chain is immobilized into only... [Pg.233]

Fig. 21. Molecular modelling (A,B) of rabbit serotransferrin glycan and (C) of human lactotransferrin [192, 210,275] (A) 3D structure of rabbit serotransferrin (B) interaction of rabbit serotransferrin glycan in a broken-wing conformation with a peptide segment (amino acids 254 to 271) in an a-helix conformation, 7,7, Al-acetylneuraminic acid residues (see Fig. 6A). (C) 3D structure of human lactotransferrin. Arrows indicate the position of glycans. Fig. 21. Molecular modelling (A,B) of rabbit serotransferrin glycan and (C) of human lactotransferrin [192, 210,275] (A) 3D structure of rabbit serotransferrin (B) interaction of rabbit serotransferrin glycan in a broken-wing conformation with a peptide segment (amino acids 254 to 271) in an a-helix conformation, 7,7, Al-acetylneuraminic acid residues (see Fig. 6A). (C) 3D structure of human lactotransferrin. Arrows indicate the position of glycans.

See other pages where Lactotransferrin rabbit is mentioned: [Pg.442]    [Pg.208]    [Pg.210]    [Pg.210]    [Pg.234]    [Pg.175]   
See also in sourсe #XX -- [ Pg.206 ]




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