β-Galactoside α-2,3-sialyltransferase
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Publisher
Springer Berlin Heidelberg
Link
http://link.springer.com/content/pdf/10.1007/978-3-540-49753-0_44.pdf
Reference17 articles.
1. Rearick, J.I.; Sadler, J.E.; Paulson, J.C.; Hill, R.L.: Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem., 254, 4444–4451 (1979)
2. Kono, M.; Ohyama, Y.; Lee, Y.C.; Hamamoto, T.; Kojima, N.; Tsuji, S.: Mouse β-galactoside α 2,3-sialyltransferases: comparison of in vitro substrate specificities and tissue specific expression. Glycobiology, 7, 469–479 (1997)
3. Sadler, J.E.; Rearick, J.I.; Paulson, J.C.; Hill, R.L.: Purification to homogeneity of a β-galactoside α2→3 sialyltransferase and partial purification of an α-N-acetylgalactosaminide α2→6 sialyltransferase from porcine submaxillary glands. J. Biol. Chem., 254, 4434–4443 (1979)
4. Chandrasekaran, E.V.; Jain, R.K.; Larsen, R.D.; Wlasichuk, K.; Matta, K.L.: Selectin ligands and tumor-associated carbohydrate structures: Specificities of a2,3-Sialyltransferases in the assembly of 3′-sialyl-6-sulfo/sialyl Lewis a and x, 3′-sialyl-6′-sulfo Lewis x, and 3′-sialyl-6-sialyl/sulfo blood group T-hapten. Biochemistry, 34, 2925–2936 (1995)
5. Shigeta, S.; Winter, H.C.; Goldstein, I.J.: α-(2→3)-and α-(2→6)-sialyltrans-ferase activities present in three variants of Ehrlich tumor cells: identifica-tion of the products derived from N-acetyllactosamine and β-D-Gal-(1→3)-α-D-GalNAc-(1→O)-Bn. Carbohydr. Res., 264, 111–121 (1994)
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