ArticleGlycoconjugate journal1999
Differences in N-acetyllactosamine synthesis between beta-1,4-galactosyltransferases I and V.
Article in Glycoconjugate journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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0 citing papers in PubMed, 10 citations in OpenAlex.
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2 authors at 1 institution in 1 country.
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Abstract
Unlike classical beta-1,4-galactosyltransferase (beta-1,4-GalT I), beta-1,4-GalT V (formerly IV**) has little activity towards 1 mM N-acetylglucosamine [Sato et al. (1998) Proc Natl Acad Sci USA 95:472-477]. The human beta-1,4-GalTs I and V were expressed individually in Sf-9 cells by transfection of the full coding sequences, and their N-acetyllactosamine synthetase activities were determined towards different N-acetylglucosamine concentrations. Kinetic studies using the cell homogenates as an enzyme source revealed that beta-1,4-GalTs I and V possess Km values of 0.6 mM and 33 mM towards N-acetylglucosamine, and of 48 microM and 41 microM towards UDP-Gal, respectively. No significant inhibition of N-acetyllactosamine synthesis with alpha-lactalbumin was observed for beta-1,4-GalT V but the significant inhibition with alpha-lactalbumin was observed for beta-1,4-GalT I.
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