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Poly sialyltransferase

Phillips, G.R., Kenshel, L.A., Crossin, K.L. Developmental expression of two rat poly-sialyltransferases that modify the neural cell adhesion molecule N-CAM. Brain Res. Dev. Brain Re.s., 1997,102, 143-155. [Pg.2013]

Sialyltransferases can be solubilized from their subcellular site by using detergents, and be purified by affinity chromatography on, for example, CDP-6-aminohexanol-agarose,267 as already described. Solubilization of frog- and rat-liver sialyltransferases by means of Triton X-100 has been described.27 Soluble sialyltransferase occurs in colostrum, and is also present in small quantities in normal blood-serum. From the latter source, the enzyme was purified 300-fold by poly (acrylamide) gel-electrophoresis.2 ... [Pg.193]

R. D. McCoy, E. R. Vimr, and F. A. Troy, CMP-NeuNAc poly-a-2,8-sialosyl sialyltransferase and the biosynthesis of poiysialosyl units in neural cell adhesion molecules, J. Biol. Chem. 260 i 2695 (1985). [Pg.503]

However, little is known about the expression of Lewis-x and sialyl-Lewis-x blood-group glycolipids with multilactosamine (or poly-lactosamine) chain-bound to ceramide. A novel sialyltransferase, SAT-3 (CMP-NeuAc nLcOse4Cer a2,3sia-lyltransferase Figure 1 Step 13), has been characterized in bovine spleen [147, 148], embryonic chicken brains [79, 130, 131], human colon carcinoma [79, 131, 132], melanoma WM266-4 cells [149], and human placenta [133]. [Pg.1456]

Cho, J. W., and Troy, F. A., 1989, Gangliosides as exogenous acceptors to map the acceptor sugar requirements of the poly-a2,8-sialyltransferase in Escherichia coli kl, Proc. Xth Int. Symp. Glycoconjugates, p. 143. [Pg.88]

Weisgerber, C., Hamsen, A., and Frosch, M., 1991, Complete nucleotide and deduced protein sequence of CMP-NeuAc poly alpha-2,8-sialyltransferase of Escherichia coli Kl, Glycobiology 1 357-366. [Pg.94]

In neuroinvasive E. coli K1, synthesis of the a2,8-linked polySia capsule is catalyzed by a CMP-Sia poly-a2,8-sialosyl sialyltransferase (polyST) complex which is postulated to carry out the following reactions ... [Pg.114]

Neither NeuE nor NeuS appears to have any relevant homology to the liver a2,3 or a2,6 sialyltransferases (Steenbergen and Vimr, 1991). Whether any homology exists between NeuE or NeuS and the eukaryotic CMP-Sia poly-a2,8-sialosyl sialyltransferase originally described in a Golgi-enriched fraction from 20-day-old fetal rat brains (McCoy et al., 1985), awaits cloning of this important mammalian enzyme. [Pg.118]

Use of the E, coli K1 Poly-a2,8-sialyltransferase to Identify Preexisting a2,8-Linked Oligo-Polysialic Acid Chains... [Pg.131]

Troy, F. A., Janas, T, and Merker, R. I., 1990c, Topology of the poly-a-2,8-sialyltransferase in E. coli Kl and energetics of polysialic acid chain translocation across the inner membrane, Glycoconj. J. 7 383. [Pg.142]

See other pages where Poly sialyltransferase is mentioned: [Pg.410]    [Pg.2004]    [Pg.2009]    [Pg.83]    [Pg.129]    [Pg.410]    [Pg.2004]    [Pg.2009]    [Pg.83]    [Pg.129]    [Pg.95]    [Pg.97]    [Pg.137]    [Pg.1219]    [Pg.1370]    [Pg.1373]    [Pg.2282]    [Pg.148]    [Pg.149]    [Pg.329]    [Pg.484]    [Pg.485]    [Pg.1337]    [Pg.1948]    [Pg.76]    [Pg.122]    [Pg.128]   
See also in sourсe #XX -- [ Pg.114 ]



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