Search results for "Galactose"

The lactose operon from Lactobacillus casei is involved in the transport and metabolism of the human milk oligosaccharide core-2 N-acetyllactosamine

2018

The lactose operon (lacTEGF) from Lactobacillus casei strain BL23 has been previously studied. The lacT gene codes for a transcriptional antiterminator, lacE and lacF for the lactose-specific phosphoenolpyruvate: phosphotransferase system (PTS) EIICB and EIIA domains, respectively, and lacG for the phospho-β-galactosidase. In this work, we have shown that L. casei is able to metabolize N-acetyllactosamine (LacNAc), a disaccharide present at human milk and intestinal mucosa. The mutant strains BL153 (lacE) and BL155 (lacF) were defective in LacNAc utilization, indicating that the EIICB and EIIA of the PTS are involved in the uptake of LacNAc in addition to lactose. Inactivation of lacG aboli…

Adaptive Processes Concerned with Absorption and Metabolism of Xylitol

1969

The turnover rate of a monosaccharide or poly alcohol in most cases depends on the mode of application. With the exception of glucose or galactose carbohydrates are metabolized faster after intravenous application than after oral application. This shows, that absorption from the gastro-intestinal tract is a rate limiting factor. Dealing with adaptive processes we therefore have to be concerned with absorptive mechanisms on one hand and enzymatic reactions in the cellular metabolism on the other hand.

Galactose increase in an infant whose mother is heterozygous for peripheral uridine diphosphate galactose‐4‐epimerase deficiency

1991

Meat allergy associated with galactosyl‐α‐(1,3)‐galactose (α‐Gal)—Closing diagnostic gaps by anti‐α‐Gal IgE immune profiling

2017

Background Glycoproteins and glycolipids of some mammalian species contain the disaccharide galactosyl-α-(1,3)-galactose (α-Gal). It is known that α-Gal is immunogenic in humans and causes glycan-specific IgG and also IgE responses with clinical relevance. α-Gal is part of the IgE-reactive monoclonal therapeutic antibody cetuximab (CTX) and is associated with delayed anaphylaxis to red meat. In this study, different α-Gal-containing analytes are examined in singleplex and multiplex assays to resolve individual sensitization patterns with IgE against α-Gal. Methods Three serum groups, α-Gal-associated meat allergy (MA) patients, idiopathic anaphylaxis (IA) patients with suspected MA, and non…

A Trisialoganglioside Containing a Sialyl α2-6 N-Acetylgalactosamine Residue Is a Cholinergic-Specific Antigen, Chol-1α1

1992

Cholinergic-specific antigens termed the Chol-1 family have been suggested to be of a ganglioside nature by Richardson et al. (J. Neurochem. 38, 1605-1614, 1982). Two molecular species of polysialogangliosides among bovine brain gangliosides were found to react with anti-Chol-1 alpha antiserum. One of them, Chol-1 alpha-a, was isolated and characterized as a trisialoganglioside containing the gangliotetraose backbone in which 1 mol of sialic acid was attached to each of the reducing end galactose, N-acetylgalactosamine and internal galactose residues, respectively. The chemical structure of Chol-1 alpha-a was determined for the first time, being as follows: IV3NeuAc III6NeuAc II3NeuAc-GgOse…

D-Galactose binding lectins from the tunicate Ascidiamalaca: Subunit characterization and hemocyte surface distribution

1988

Abstract D-galactose specific lectins purified from Ascidia malaca serum contain a major protein component with an apparent molecular weight of about 58,000 daltons, which moves more rapidly under non-reducing conditions. Intramolecular disulfide linkages can explain this behaviour, suggesting a compact protein structure. Membrane lectins have been demonstrated on the surface of about 34% hemocytes by immunofluorescent methods using a rabbit antiserum against the isolated serum lectins. Small, medium and large hemocytes can be positive, as also shown by binding on Sepharose spherules or by rosette formation with sheep and rabbit erythrocytes. Binding is inhibited by the same sugars specific…

On the role of D-glucuronic acid in the aggregation of cells from the marine sponge Geodia cydonium.

1979

Abstract The aggregation receptor (AR) from the marine sponge GEODIA CYDONIUM was analyzed with respect to its monosaccharide composition. Three major sugars ( D -galactose, D -glucose and D -glucuronic acid) accounted for about 85 % of the total carbohydrate. Negative results with different lectins directed against D -galactosyl, N -acetyl- D -galactosaminyl and N -acetyl- D -glucosaminyl groups, respectively, showed that these sugars are serologically unreactive in AR. Positive serological reactions were obtained with CONCANAVALIN A and LIMULUS POLYPHEMUS agglutinin. AR also reacted strongly with the basic polymer poly- L -lysine. Reaggregation experiments performed on the basis of these …

NOVEL COMPOSED GALACTOSYLATED NANODEVICES CONTAINING A RIBAVIRIN PRODRUG AS HEPATIC CELL-TARGETED CARRIERS FOR HCV TREATMENT

2013

In this paper, we describe the preparation of liver-targeted nanoparticles potentially able to carry to hepatocytes a ribavirin (RBV) prodrug, exploiting the presence of carbohydrate receptors in the liver (i.e., ASGPR in hepatocytes). These particles were obtained starting from a galactosylated phospholipid-polyaminoacid conjugate. This latter was obtained by chemical reaction of ALPHA, BETA -poly(N-2-hydroxyethyl) (2-aminoethylcarbamate)-DL-aspartamide (PHEA-EDA) with 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine-N-(succinyl) sodium salt (DPPE), and subsequent reaction with lactose, obtaining PHEA-EDA-DPPE-GAL copolymer. To enhance the entrapment into obtained nanostructures, a hydroph…

Stereoselective synthesis of benzomorphan derivatives with perpivaloylated galactose as the chiral auxiliary.

2006

Physicochemical and functional characterization of the polymerization process of the Geodia cydonium lectin

1985

The extracellularly localized, galactose-specific lectin from the sponge Geodia cydonium binds at one class of sites, 40 mol Ca2+/mol lectin with an association constant (Ka) of 0.3 X 10(6)M-1. Stoichiometric calculations reveal that in the extracellular milieu 22 mol Ca2+ (maximum) are complexed per mol lectin. Binding of Ca2+ to the lectin increases its apparent Mr from 44000 to 56000 (electrophoretic determination) or from 36500 to 53500 (high-pressure liquid gel chromatographical determination); the s20, w increases from 4.3 S to 4.5 S if Ca2+ is added to the lectin. In the presence of Ca2+ the lectin undergoes a conformational change perhaps by expanding the carbohydrate side chains wh…