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A-Acetyllactosamine structures

An enzyme which transfers the a-Gal residue to A-acetyllactosamine structures in the glycoproteins of mammals other than humans has attracted attention because the a-Gal/)-(1 3)-Gal epitope is a major obstacle to the use of organs from other mammals in xenotransplantation because of the... [Pg.438]

Fig. 2. iV-glycans of the hybrid type. A triantennary structure with sialylated Af-acetyllactosamine (LacNAc) building blocks B biantennary structure with sialylated or fucosylated poly-LacNAc building blocks. The N-glycan core structure is written in bold letters... [Pg.95]

H Chemical Shifts of Structural-reporter Groups of Constituent Monosaccharides for Asialo Di-, Tri-, and Tetra-antennary Glycopeptides of the A-Acetyllactosamine Type (Compounds 8, 9, and 13)... [Pg.239]

Therefore, the simplest explanation for the action of a-lactalbumin and galactosyltransferase, as suggested by Browne et al. (1969), is that a-lactalbumin, in complexing with galactosyltransferase, modifies the conformational structure of the latter to produce a form of the enzyme that more readily catalyzes the production of lactose, and then does so in preference to A -acetyllactosamine. [Pg.255]

Rat mammary-gland transferrin. Rat milk transferrin contains four glycovari-ants that differ only in their sialic acid content. The primary structure of the two major variants has been determined by Escriva et al. [67]. As shown in Fig. 8D, the glycoforms contain either one or two A-acetylneuraminic acid residues a-2,6-linked to galactose in a conventional diantennary glycan of the A-acetyllactosaminic type. Most contain fucose a-l,6-linked to the proximal A-acetylglucosamine residue. [Pg.229]

The X-ray structure of a diantennary octasaccharide of the A-acetyllactosamine type complexed to isolectin I from Lathyrus ochrus at 2.3 A resolution was solved [53]. The complex is stabilized by numerous hydrogen bonds, many also involving water molecules. Van der Waals interactions, including some with aromatic residues are also involved. It is apparent that GlcNAc((3l-2)Man residues play an important role in the oligosaccharide-lectin interaction. [Pg.410]


See other pages where A-Acetyllactosamine structures is mentioned: [Pg.1301]    [Pg.1307]    [Pg.1742]    [Pg.2009]    [Pg.154]    [Pg.1301]    [Pg.1307]    [Pg.1742]    [Pg.2009]    [Pg.154]    [Pg.73]    [Pg.335]    [Pg.337]    [Pg.295]    [Pg.404]    [Pg.1751]    [Pg.1752]    [Pg.1752]    [Pg.1755]    [Pg.2465]    [Pg.295]    [Pg.298]    [Pg.312]    [Pg.341]    [Pg.259]    [Pg.538]    [Pg.634]    [Pg.431]    [Pg.439]    [Pg.2]    [Pg.65]    [Pg.65]    [Pg.191]    [Pg.194]    [Pg.214]    [Pg.219]    [Pg.228]    [Pg.229]    [Pg.229]    [Pg.230]    [Pg.573]    [Pg.574]    [Pg.580]    [Pg.128]    [Pg.143]    [Pg.339]    [Pg.371]   


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