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Gene Review

BF4249  -  endo-beta-galactosidase

Bacteroides fragilis YCH46

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Disease relevance of BF4249

  • It could be converted to a sharper band (apparent Mr 23000) by treatment with endo-beta-galactosidase from Bacteroides fragilis and so probably contains one or more sites at which an oligosaccharide of the poly(N-acetyl-lactosamine) type is attached [1].

High impact information on BF4249


Chemical compound and disease context of BF4249


Anatomical context of BF4249

  • Embryos cultured in the presence of endo-beta-galactosidase from the 2- to 4-cell stage onwards, or treated with the enzyme at the compacting 8-cell stage, continued to compact and proceeded to form blastocysts at the normal rate [10].

Associations of BF4249 with chemical compounds

  • Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of N-acetyllactosamine-repeating oligosaccharide beta-glycosides using its transglycosylation activity [11].
  • Novel chromogenic substrates for endo-beta-galactosidase were designed on the basis of the structural features of keratan sulfate [11].
  • A colorimetric assay for endo-beta-galactosidase was developed using the synthetic substrates on the basis of the determination of p-nitrophenol liberated from GlcNAcbeta-pNP or Glcbeta-pNP formed by the enzyme through a coupled reaction involving beta-N-acetylhexosaminidase (beta-NAHase) or beta-d-glucosidase [11].
  • On the assumption that recompaction and de novo compaction occur by similar mechanisms, we propose that carbohydrate-binding molecules are involved which have high affinities for poly-N-acetyllactosamine structures and protect them from digestion by endo-beta-galactosidase [10].

Analytical, diagnostic and therapeutic context of BF4249


  1. Proteolytic and chemical dissection of the human erythrocyte glucose transporter. Cairns, M.T., Elliot, D.A., Scudder, P.R., Baldwin, S.A. Biochem. J. (1984) [Pubmed]
  2. Structures of neutral O-linked polylactosaminoglycans on human skim milk mucins. A novel type of linearly extended poly-N-acetyllactosamine backbones with Gal beta(1-4)GlcNAc beta(1-6) repeating units. Hanisch, F.G., Uhlenbruck, G., Peter-Katalinic, J., Egge, H., Dabrowski, J., Dabrowski, U. J. Biol. Chem. (1989) [Pubmed]
  3. Endo-beta-D-galactosidases of Bacteroides fragilis and Escherichia freundii hydrolyze linear but not branched oligosaccharide domains of glycolipids of the neolacto series. Scudder, P., Hanfland, P., Uemura, K., Feizi, T. J. Biol. Chem. (1984) [Pubmed]
  4. Human serum contains a novel beta 1,6-N-acetylglucosaminyltransferase activity that is involved in midchain branching of oligo (N-acetyllactosaminoglycans). Leppänen, A., Penttilä, L., Niemelä, R., Helin, J., Seppo, A., Lusa, S., Renkonen, O. Biochemistry (1991) [Pubmed]
  5. 500 MHz 1H n.m.r. of oligosaccharides of N-acetyl-lactosamine-type released from human erythrocyte glycopeptides by endo-beta-galactosidase. Hounsell, E.F., Feeney, J., Scudder, P. Biochem. J. (1988) [Pubmed]
  6. Isolation and characterization of an endo-beta-galactosidase from Bacteroides fragilis. Scudder, P., Uemura, K., Dolby, J., Fukuda, M.N., Feizi, T. Biochem. J. (1983) [Pubmed]
  7. Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. Hokke, C.H., Bergwerff, A.A., Van Dedem, G.W., Kamerling, J.P., Vliegenthart, J.F. Eur. J. Biochem. (1995) [Pubmed]
  8. Characterisation of oligosaccharides released from human-blood-group O erythrocyte glycopeptides by the endo-beta-galactosidase of Bacteroides fragilis. A study of the enzyme susceptibility of branched poly(N-acetyllactosamine) structures. Scudder, P., Lawson, A.M., Hounsell, E.F., Carruthers, R.A., Childs, R.A., Feiz, T. Eur. J. Biochem. (1987) [Pubmed]
  9. New method for the isolation of polyglycosylceramides from human erythrocyte membranes. Miller-Podraza, H., Andersson, C., Karlsson, K.A. Biochim. Biophys. Acta (1993) [Pubmed]
  10. Cell interactions in preimplantation embryos: evidence for involvement of saccharides of the poly-N-acetyllactosamine series. Rastan, S., Thorpe, S.J., Scudder, P., Brown, S., Gooi, H.C., Feizi, T. Journal of embryology and experimental morphology. (1985) [Pubmed]
  11. Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of N-acetyllactosamine-repeating oligosaccharide beta-glycosides using its transglycosylation activity. Murata, T., Hattori, T., Amarume, S., Koichi, A., Usui, T. Eur. J. Biochem. (2003) [Pubmed]
  12. Isolation and characterization of sulphated oligosaccharides released from bovine corneal keratan sulphate by the action of endo-beta-galactosidase. Scudder, P., Tang, P.W., Hounsell, E.F., Lawson, A.M., Mehmet, H., Feizi, T. Eur. J. Biochem. (1986) [Pubmed]
  13. Tk polyagglutination produced in vitro by an endo-beta-galactosidase. Doînel, C., Andreu, G., Cartron, J.P., Salmon, C., Fukuda, M.N. Vox Sang. (1980) [Pubmed]
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