Просмотр исходного текста страницы Ligands-Inhibition-Assay-Le-Ii-Lnfp-Potent-Times-X-Pentasaccharide-Lnfp-Iii-Sialyl-Le-X-Man-Gal-Galnac-Inactive-p

The decreasing order of PA-IIL affinity for the oligosaccharides tested was Le(a) pentaose or = sialyl Le(a) tetraose methyl alphaFuc Fuc and Fucalpha1-2Gal (H disaccharide) [http://allinno.com/product/healthcare/671.html 2'-fucosyllactose] (H trisaccharide), Le(x) pentaose, Le(b) hexaose I)Le(x) trisaccharide (Galbeta1-4[Fucalpha1-3]GlcNAc) sialyl Le(x) trisaccharide Man Gal, GalNAc, and Glc (inactive). The results presented here, in accordance with the crystal 3D structural data, imply that the combining site of PA-IIL is a small cavity-type best fitting Fucalpha1- with a specific shallow groove subsite for the remainder part of the Le(a) saccharides, and that polyvalent glycotopes enhance the reactivity. The Fuc Man Ralstonia solanacearum lectin RSL, which resembles PA-IIL in sugar specificity, differs from it in it's better fit to the B and A followed by H oligosaccharides vs. Fuc, whereas, the second R. solanacearum lectin RS-IIL (the structural homologue of PA-IIL) binds Man Fuc. These results provide a valuable information on PA-IIL interactions with mammalian glycoforms and the possible spectrum of attachment sites for the homing of this aggressive bacterium onto the target molecules.<br /><br /> Such information might be useful for the antiadhesive therapy of P. Effect of albumin on amylase assay using blue starch polymer.The nature of the stimulation by albumin of amylase activity determined by use of blue starch polymer was studied. The binding of albumin to the starch polymer was responsible for the stimulation of amylase activity, since the stimulation was observed with the albumin-bound blue starch polymer as substrate irrespective of the presence or absence of free albumin in the reaction mixture. When the albumin-bound blue starch polymer was hydrolysed by amylase, the blue oligosaccharide fragments were released with the albumin attached. These oligosaccharide fragments were about 1 times larger in average molecular size than the fragments released in the absence of albumin, suggesting that the apparent stimulation of amylase by albumin, (about 1 times) is due to the liberation of the larger oligosaccharide fragments.Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1.<br /><br />To examine [https://en.wikipedia.org/wiki/2%27-Fucosyllactose Seebio 2'-Fucose lactose] to which protein structure and tissue-type influence glycosylation, we have determined the oligosaccharide structures at each of the three glycosylation sites (Asn-23, 74 and 98) of the cell surface glycoprotein Thy-1 isolated from rat brain and thymus. The results show that there is tissue-specificity of glycosylation and that superimposed on this is a significant degree of site-specificity. On the basis of the site distribution of oligosaccharides, we find that no Thy-1 molecules are in common between the two tissues despite the amino acid sequences being identical. We suggest, therefore, that by controlling N-glycosylation a tissue creates an unique set of glycoforms disposition). The structures at each of the three sites were also determined for the thymocyte Thy-1 that binds to lentil lectin (Thy-1 L+) and for that which does not (Thy-1 L-). Segregation of intact thymus Thy-1 into two distinct sets of glycoforms by lentil lectin was found to be due to the structures at site 74. Analysis of oligosaccharide structures at the 'passenger' sites (23 and 98) suggests that either Thy-1 L+ and Thy-1 L- molecules are made in different cell-types or that the biosynthesis of oligosaccharides at one site is influenced by the glycosylation at other sites.<br /><br />DOI 2j4-75987.t2359.xSynthesis of 2-C-branched oligo(glyco-amino acid)s (OGAAs) by ring opening of 1,2-cyclopropanecarboxylated sugar donors.Host-dependent variation of asparagine-linked oligosaccharides at individual glycosylation sites of Sindbis virus glycoproteins.We examined the Asn-linked oligosaccharides at individual glycosylation sites of the two envelope glycoproteins of Sindbis virus, E1 and E2. The analysis was done by separating tryptic glycopeptides by reverse phase high performance liquid chromatography and analyzing the oligosaccharides from isolated glycopeptides by gel filtration chromatography. Both E1 and E2 have two glycosylation sites each in virus grown in chick embryo fibroblasts, baby hamster kidney cells, and Chinese hamster ovary cells.