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Biosynthesis of terminal Gal alpha 1—-3Gal beta 1—-4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide alpha 1—-3-galactosyltransferase from calf thymus.
Open accessAbstract
A UDP-Gal:Gal beta 1----4GlcNAc-R alpha 1----3- and a UDP-Gal:GlcNAc-R beta 1----4-galactosyltransferase have been purified 44,000- and 101,000-fold, respectively, from a Triton X-100 extract of calf thymus by affinity chromatography on UDP-hexanolamine-Sepharose and alpha-lactalbumin-Sepharose in a yield of 25-40%. Sodium dodecyl sulfate gel electrophoresis under reducing conditions revealed a major polypeptide species with a molecular weight of 40,000 and a minor form at Mr 42,000 for the alpha 1----3-galactosyltransferase and a major polypeptide with Mr 51,000 for the beta 1----4-galactosyltransferase. Analytical gel filtration on Sephadex G-100 yielded a monomeric form for each of the galactosyltransferases with Mr 43,000 and 59,000 respectively, in addition to peaks of activity at higher molecular weights. Isoelectric focussing of the alpha 1----3-galactosyltransferase revealed a significant charge heterogeneity with forms varying in pI values between 5.0 and 6.5. Acceptor specificity studies indicated that the purified alpha 1----3-galactosyltransferase was free from contaminating galactosyltransferase activities such as those involved in the synthesis of Gal beta 1----4GlcNAc-R and Gal beta 1----3GalNAc-R sequences, the blood group B determinant, the Pk antigen, trihexosylceramide, and ganglioside GM1. The alpha 1----3-galactosyltransferase appeared to be highly active with glycoproteins, oligosaccharides, and glycolipids having a terminal Gal beta 1----4GlcNAc beta 1----unit such as asialo-alpha 1-acid glycoprotein (Km = 1.25 mM), Gal beta 1----4GlcNAc beta 1----2Man alpha 1----3Man beta 1----4GlcNAc (Km = 0.57 mM), and paragloboside. The action of the alpha 1----3-galactosyltransferase was found to be mutually exclusive with that of the NeuAc:Gal beta 1----4GlcNAc-R alpha 2----6-sialyltransferase from bovine colostrum. In addition alpha 1----3-fucosylation of the N-acetylglucosamine residue in the preferred disaccharide acceptor structure completely blocked galactosylation of the alpha 1----3-galactosyltransferase.
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Citations
Cited by
Galili, U., Shohet, S. B., Kobrin, E., Stults, C. L., & Macher, B. A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77900-9 · Cited by 817
Galili, U., Clark, M. R., Shohet, S. B., Buehler, J., & Macher, B. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.5.1369 · Cited by 549
Macher, B. A., & Galili, U. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.11.003 · Cited by 404
The α-gal epitope (Galα1-3Galβ1-4GlcNAc-R) in xenotransplantation
Galili, U. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01294-9 · Cited by 212
Bouhours, D., Pourcel, C., & Bouhours, J.-F. (1996) · Glycoconjugate Journal · doi:10.1007/bf01053190 · Cited by 113
Metadata
- Authors
- Blanken, W. M., & Van den Eijnden, D. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1985-10
- Volume
- 260
- Issue
- 24
- Pages
- 12927-12934
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1812801726
- Cited by
- 175
- References
- 0
- FWCI
- 2.33
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Biosynthesis of terminal Gal alpha 1—-3Gal beta 1—-4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide alpha 1—-3-galactosyltransferase from calf thymus. https://app.cochat.ai/papers/10.1016/s0021-9258(17)38814-2
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- Blanken, W. M., & Van den Eijnden, D. H. (1985). Biosynthesis of terminal Gal alpha 1—-3Gal beta 1—-4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide alpha 1—-3-galactosyltransferase from calf thymus. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)38814-2
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