Results 101 to 110 of about 2,030 (160)
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Hydrophobic chromatography of galactosyltransferase
Archives of Biochemistry and Biophysics, 1976Abstract O-Glycosidic analogs of N-acetylglucosamine are good substrates for galactosyltransferase, and as the O-substituted group becomes more hydrophobic, the apparent Km decreases as much as 2000-fold. l -leucine, leucine-amide, norleucine, valine, ϵ-amino-n-caproic acid and tyrosine-agaroses all retain galactosyltransferase in the presence of 1 ...
C R, Geren, S C, Magee, K E, Ebner
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Biochimica et Biophysica Acta (BBA) - General Subjects, 1999
Enzymatic glycosylation of proteins and lipids is an abundant and important biological process. A great diversity of oligosaccharide structures and types of glycoconjugates is found in nature, and these are synthesized by a large number of glycosyltransferases. Glycosyltransferases have high donor and acceptor substrate specificities and are in general
Amado, M. +3 more
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Enzymatic glycosylation of proteins and lipids is an abundant and important biological process. A great diversity of oligosaccharide structures and types of glycoconjugates is found in nature, and these are synthesized by a large number of glycosyltransferases. Glycosyltransferases have high donor and acceptor substrate specificities and are in general
Amado, M. +3 more
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The galactosyltransferase family
Cellular and Molecular Life Sciences (CMLS), 2002Galactose is transferred via several linkages to acceptor structures by galactosyltransferase enzymes. In prokaryotes, galactose is mainly found on lipopolysaccharides and capsular polysaccharides. In eukaryotes, galactosyltransferases, which are localized in the Golgi apparatus, are involved in the formation of several classes of glycoconjugates and ...
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A pH-sensitive assay for galactosyltransferase
Analytical Biochemistry, 2004We report here a new pH-indicator-based assay for galactosyltransferase. The method is simple and fast, requires no specialized equipment, labeled substrate, or other expensive materials, and is thus expected to have broad applications including automated high-throughput screening.
Chenghua, Deng, Rachel R, Chen
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β-Glucosylation of chitooligomers by galactosyltransferase
Carbohydrate Research, 1997Galactosyltransferase from bovine milk was found to be able to utilise UDP-Glc to transfer Glc onto GlcNAc and chitooligomers[-beta-GlcNAc-(1-->4)-]n, n = 2-4. beta-Glucosylated products were used in binding studies with NKR-P1A protein cloned from rat natural killer cells.
V, Kren +6 more
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Galactosyltransferase—still up and running
Biochimie, 2003The following review on galactosyltransferase (gal-T1) intends to cover genetic, biochemical, structural, biotechnological, cell biological and medical aspects of this enzyme in a comprehensive manner from discovery to the present day which have brought to light a genetic defect of this enzyme.
Berger EG, Rohrer J
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A Cancer-Associated Galactosyltransferase Isoenzyme
New England Journal of Medicine, 1978GALACTOSYLTRANSFERASE has been studied in human serum, and early reports failed to demonstrate an elevation of total serum galactosyltransferase in malignant disease.1 , 2 Subsequent electrophoretic studies from this laboratory revealed that, although the majority of the serum enzyme runs as a single broad peak on polyacrylamide gels, serum specimens ...
D K, Podolsky +3 more
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Studies on the inhibition of sialyl- and galactosyltransferases
Glycoconjugate Journal, 1997The inhibition of the alpha-2,6-sialyltransferase from rat liver, the alpha-2,3-sialyltransferase from porcine submandibular gland and of the galactosyltransferase from human milk were studied using monosaccharide-, nucleoside- and nucleotide-derivatives of their naturally occurring donor substrates cytidine 5'-monophosphate-N-acetylneuraminic acid and
R G, Kleineidam +3 more
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2002
The enzyme β4-galactosyltransferase-I (β4GalT-I; UDP-Gal:GlcNAc β4-galactosyltransferase; EC 2.4.1.38) is a constitutively expressed, trans-Golgi resident, type II membrane-bound glycoprotein that is widely distributed in vertebrates. The protein domain structure established for β4GalT-I consists of: (1) a short NH2-terminal cytoplasmic domain of 11 or
Nancy L. Shaper, Joel H. Shaper
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The enzyme β4-galactosyltransferase-I (β4GalT-I; UDP-Gal:GlcNAc β4-galactosyltransferase; EC 2.4.1.38) is a constitutively expressed, trans-Golgi resident, type II membrane-bound glycoprotein that is widely distributed in vertebrates. The protein domain structure established for β4GalT-I consists of: (1) a short NH2-terminal cytoplasmic domain of 11 or
Nancy L. Shaper, Joel H. Shaper
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The α1,3-Galactosyltransferase Gene
1999Cell surface glycoconjugates (glycoproteins and glycolipids) are well positioned topologically to be involved in cell-cell interactions and transmembrane signaling. Their glycans (sugar chains) protrude from the surface, and display considerable structural complexity.
David H. Joziasse +2 more
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