scholarly journals The lactose and galactose content of milk fats and suitability for galactosaemia

2015 ◽  
Vol 5 ◽  
pp. 42-43 ◽  
Author(s):  
P.A. Portnoi ◽  
A. MacDonald
Keyword(s):  
Galactose Content

UDP-D-glucose 4-epimerase activity of the tissue culture of white poplars (Populus alba L. var. pyramidalis)

1982 ◽  
Vol 47 (5) ◽  
pp. 1530-1536 ◽  
Author(s):  
Ladislav Bilisics ◽  
Štefan Karácsonyi ◽  
Marta Kubačková
Keyword(s):  
Tissue Culture ◽  
Cell Walls ◽  
Enzyme Preparation ◽  
Uridine Diphosphate ◽  
Populus Alba ◽  
Activity Change ◽  
White Poplar ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Galactose Content

The presence of UDP-D-glucose 4-epimerase (EC 5.1.3.2) in the culture tissue of white poplar was evidenced. As found, the partially purified enzyme preparation contained UDP-D-glucose glucosyltransferase, UDP-D-galactose galactosyltransferase and non-specific enzymes able to cleave the uridine-diphosphate saccharides into the appropriate hexose monophosphates. The activity change of UDP-D-glucose 4-epimerase in tissue culture cells during the growth was in accord with changes in D-galactose content in cell walls and indicated the possibility to regulate the formation of polysaccharides containing D-galactose at the level of production of UDP-D-galactose in cells.

scholarly journals Fucose content of keratan sulphates from bovine articular cartilage

1991 ◽  
Vol 273 (2) ◽  
pp. 307-310 ◽  
Author(s):  
G H Tai ◽  
G M Brown ◽  
H G Morris ◽  
T N Huckerby ◽  
I A Nieduszynski
Keyword(s):  
Molecular Weight ◽  
Articular Cartilage ◽  
Molecular Size ◽  
Gel Permeation Chromatography ◽  
Repeat Sequence ◽  
Keratan Sulphate ◽  
Bovine Articular Cartilage ◽  
Gel Permeation ◽  
Fucose Content ◽  
Galactose Content

Alkaline-borohydride-reduced keratan sulphate chains were isolated from bovine articular cartilage (6-8-year-old animals). Nine keratan sulphate fractions of increasing molecular weight were prepared by gel-permeation chromatography on a calibrated column of TSK 30 XL. The samples were analysed for fucose and galactose contents (% by wt. of keratan sulphate) and fucose/galactose ratio. The fucose content increased with molecular size, but the galactose content remained constant. It was concluded that the alpha(1→3)-linked fucose [Thornton, Morris, Cockin, Huckerby, Nieduszynski, Carlstedt, Hardingham & Ratcliffe (1989) Biochem. J. 260, 277-282] was located within the poly-N-acetyl-lactosamine repeat sequence of articular-cartilage keratan sulphate.

Preparation and Utilization of a Biosensor Based on Galactose Oxidase

1992 ◽  
Vol 57 (11) ◽  
pp. 2287-2294 ◽  
Author(s):  
Eva Vrbová ◽  
Jitka Pecková ◽  
Miroslav Marek
Keyword(s):  
Oxygen Sensor ◽  
Specific Activity ◽  
Galactose Oxidase ◽  
Collagen Membrane ◽  
Michaelis Constant ◽  
Nylon Mesh ◽  
Native Collagen ◽  
The Stability ◽  
Galactose Content

An enzyme electrode for D-galactose determination was prepared by fixation of a carrier with immobilized galactose oxidase (E.C. 1.1.3.9) or coimmobilized galactose oxidase and catalase (E.C. 1.11.1.6) to a Clark-type oxygen sensor. The enzymes were immobilized either on a partially hydrolyzed nylon mesh or on a native collagen membrane using the Ugi reaction with cyclohexyl isocyanide and glutaraldehyde. The biosensors were characterized by the specific activity of the immobilized galactose oxidase, the apparent Michaelis constant KM(app.), and the stability expressed by time and a number of the performed analyses. The substrate specificity of the biosensor and the effect of pH and temperature of the reaction mixture on the response magnitude were also tested. The prepared biosensor was used for the determination of D-galactose content in samples of blood plasma and serum of patients with suspected galactosemia.

GALACTOSE CONTENT OF FOODS FOR GALACTOSÆMIC INFANTS

The Lancet ◽  
1962 ◽  
Vol 280 (7263) ◽  
pp. 994
Author(s):  
A. Holzel ◽  
G.M. Komrower
Keyword(s):  
Galactose Content

Effects of temperature and tissue age on gel strength and composition of agar from Gracilaria tikvahiae (Rhodophyceae)

1984 ◽  
Vol 62 (8) ◽  
pp. 1665-1670 ◽  
Author(s):  
James S. Craigie ◽  
Zong C. Wen
Keyword(s):  
Gel Strength ◽  
Wild Type ◽  
Gracilaria Tikvahiae ◽  
Morphological Mutants ◽  
Wild Type Clone ◽  
Effects Of Temperature ◽  
Lateral Branches ◽  
Increasing Temperature ◽  
Strong Inverse Relationship ◽  
Galactose Content

Agars were prepared from a wild type and two morphological mutants of Gracilaria tikvahiae grown at 17, 22, and 27 °C, and from apical segments, main axis segments, and lateral branches of the wild type clone MP-2 grown at 17 and 27 °C. The yield of native agar was 9–11% from the young parts and 19–23% from the most mature parts of the MP-2 thallus. The gel strengths of alkali-modified agars showed a strong inverse relationship with increasing temperature of growth in each of the three clones examined. The modified agar produced from plants grown at high temperature contained more sulfate and less 3,6-anhydro-L-galactose than agars produced at lower temperatures. The increase in 4-O-methyl-L-galactose content of the agars as the growth temperature increased was especially marked. Dissection experiments on clone MP-2 showed that agar with the maximum gel strength and 3,6-anhydro-L-galactose content and the minimum sulfate and 4-O-methyl-L-galactose content was produced at low temperature by apical segments and young lateral branches. The poorest quality agar was prepared from mature segments of the thallus, especially those grown at high temperatures. Agars prepared from mature parts of the thallus were greatly enriched in 4-O-methyl-L-galactose, which reached 8.8% of the weight of the agar at 27 °C. Changes in 6-O-methyl-D-galactose were smaller, but this sugar was lowest in agar prepared from young tissues of plants grown at 17 °C.

scholarly journals High Molecular Weight Proteins ofTrypanosoma cruziReduce Cross-Reaction withLeishmaniaspp. in Serological Diagnosis Tests

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Alejandra Yunuen Cervantes-Landín ◽  
Ignacio Martínez ◽  
Muslim Schabib ◽  
Bertha Espinoza
Keyword(s):  
Molecular Weight ◽  
Western Blot ◽  
High Molecular Weight ◽  
Essential Role ◽  
Serological Diagnosis ◽  
Parasitic Diseases ◽  
High Molecular Weight Proteins ◽  
Triton X ◽  
Sera Samples ◽  
Galactose Content

Chagas disease is caused by the parasiteTrypanosoma cruzi. Because of its distribution throughout Latin America, sometimes it can overlap with other parasitic diseases, such as leishmaniasis, caused byLeishmaniaspp. This might represent a problem when performing serological diagnosis, because both parasites share antigens, resulting in cross-reactions. In the present work we evaluated Mexican sera samples: 83.8% of chagasic patients recognized at least one antigen of high molecular weight (>95 kDa) when evaluated by Western blot. Proteins of 130 kDa and 160 kDa are predominantly being recognized by asymptomatic chagasic patients. When the proteins were extracted using Triton X-100 detergent, a larger number of specificT. cruziproteins were obtained. This protein fraction can be used to increase specificity to 100% in Western blot assays without losing sensitivity of the test. High molecular weight proteins ofT. cruziinclude glycoproteins with a great amount ofαMan (α-mannose),αGlc (α-glucose), GlcNAc (N-acetylglucosamine), andαGal (α-galactose) content and these structures play an essential role in antigens recognition by antibodies present in patients’ sera.

scholarly journals Permanent exposure of mucin-secreting HT-29 cells to benzyl-N-acetyl-α-D-galactosaminide induces abnormal O-glycosylation of mucins and inhibits constitutive and stimulated MUC5AC secretion

1998 ◽  
Vol 334 (1) ◽  
pp. 283-295 ◽  
Author(s):  
Sylviane HENNEBICQ-REIG ◽  
Thécla LESUFFLEUR ◽  
Calliope CAPON ◽  
Carmen de BOLOS ◽  
Isabelle KIM ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Mrna Expression ◽  
Drug Exposure ◽  
Fold Increase ◽  
Ultrastructural Level ◽  
T Antigen ◽  
Mucus Layer ◽  
Altered Regulation ◽  
Ht 29 ◽  
Galactose Content

Previous work has shown that treatment of HT-29 methotrexate (MTX) cells with benzyl-N-acetyl-α-d-galactosaminide results in profound changes in mucin oligosaccharide chains. To analyse in depth the effect of this drug, we first determined the structure of mucin oligosaccharide chains synthesized by HT-29 MTX cells and the changes induced by permanent drug exposure. Mucins from untreated cells contained nine monosialylated structures (core types 1, 2, 3 and 4) and four disialylated structures (types 1, 2 and 4). Core 1 structures predominated, in particular NeuAcα2–3Galβ1–3GalNAc-ol. Exposure of HT-29 MTX cells to benzyl-N-acetyl-α-d-galactosaminide from days 2–21 resulted in a decrease in intracellular mucins and both their sialic acid and galactose content, and an increased T (Galβ1–3GalNAcα-O-Ser/Thr) and Tn (GalNAcα-O-Ser/Thr) antigenicity. A 3-fold increase in both Galβ1–3GalNAc α2,3-sialyltransferase activity and mRNA expression was detected. At the ultrastructural level, T-antigen was not detectable in mucin droplets in control cells, but was strongly expressed in intracytoplasmic vesicles in treated cells. In these cells, MUC1 and MUC3 transcripts were up-regulated, whereas MUC2, MUC5B and MUC5AC were down-regulated. Furthermore, constitutive and secretagogue-induced MUC5AC secretion was reduced and no mucus layer was detected. In conclusion, benzyl-N-acetyl-α-d-galactosaminide induces abnormal O-glycosylation and altered regulation of MUC5AC secretion.

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