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PubMed1975

Galactose tolerance studies of individuals with reduced galactose pathway activity.

The galactose tolerance of individuals with mutant genotypes affecting the activities of galactokinase (GALK) and galactose-1-phosphate uridylyltransferase (GALT) was examined. Genotypes studied were heterozygotes for the GALK and GALT forms of galactosemia, the Duarte-variant GALT, and Philadelphia-variant GALK alleles. The measurements used were urinary concentration of galactose during pregnancy in adults and in infants from the newborn period through the first 5 months of life; the rate of elimination of an intravenous infusion of galactose; and slit-lamp examination of the lens for evidence of cataracts. No unusual urinary excretions of galactose were noted in any of the age groups studied. Intravenous galactose tolerance tests were normal in all but two women, a mother and daughter heterozygous for the GALK-deficient form of galactosemia (GALKG/GALKA). Six other GALKG/GALKA subjects had normal tolerance studies. The intrafamilial consistency and interfamilial differences in the galactose tolerance of GALKG/GALKA individuals suggest heterogeneity of the genes responsible for the GALK-deficient form of galactosemia. Although subclinical cataracts were observed in several individuals, their significance relative to the mutant genotype cannot be resolved with the available data.

Cataract↗
PubMed1998

Determination of galactose and galactocerebroside using a galactose oxidase column and electrochemical detector.

A method has been developed to measure galactose and galactocerebroside using galactose oxidase immobilized on a solid resin. Galactose oxidase converts galactose and galactocerebroside to their corresponding aldehydes and hydrogen peroxide, the latter being electroactive and measurable by electrochemical detection using DC amperometric detection. The minimal detection limits of galactose and galactocerebroside were 1 and 2 microM, respectively. The linear response to galactose and galactocerebroside was to at least 300 microM. About 100 samples can be measured per hour using flow injection analysis. The activity of sulfatidase (cerebroside-3-sulfate-3-sulfohydrolase), which converts sulfatide (sulfogalactocerebroside) to galactocerebroside, was measured, and its inhibition by O-phospho-L-tyrosine was determined.

Biosensing Techniques↗
PubMed1995

Enzymic transfer of 6-modified D-galactosyl residues: synthesis of biantennary penta- and hepta-saccharides having two 6-deoxy-D-galactose residues at the nonreducing end and evaluation of 6-deoxy-D-galactosyl transfer to glycoprotein using bovine beta-(1-->4)-galactosyltransferase and UDP-6-deoxy-D-galactose.

UDP-6-Deoxy-D-galactose and UDP-6-deoxy-6-fluoro-D-galactose were synthesized and their transfer to 2-acetamido-2-deoxy-D-glucose (N-acetyl-D-glucosamine) by beta-(1-->4)-galactosyltransferase was examined. The transfer rates of 6-deoxy-D-galactose and 6-deoxy-6-fluoro-D-galactose were 1.3 and 0.2% of that of D-galactosyl transfer, respectively. The 2-acetamido-4-O-(6-deoxy-beta-D-galactopyranosyl)-2-deoxy-D-glucopyranose (6'-deoxy-N-acetyllactosamine) and methyl 2-acetamido-4-O-(6-deoxy-6-fluoro-beta-D-galactopyranosyl)-2-deoxy-D- glucopyranoside (6'-deoxy-6'-fluoro-N-acetyllactosamine) were synthesized enzymatically in 30 and 59% yields, respectively. Further, 6-deoxy-D-galactose could be completely transferred to N-linked type biantennary oligosaccharides having two N-acetyl-D-glucosaminyl residues at the nonreducing end to give the corresponding penta- and hepta-saccharides in 55 and 57% yields, respectively. An assay of 6-deoxy-D-galactosyl transfer using asialo agalacto alpha 1-acid glycoprotein as an acceptor suggested that 6-deoxy-D-galactose was transferred to about 30% of the N-acetyl-D-glucosaminyl residues in the N-linked oligosaccharides of the glycoprotein.

Acetylglucosamine↗
PubMed1981

Galactose and galactose-1-phosphate spot test for galactosemia screening.

A simple spot test to measure galactose and galactose-1-phosphate in blood-impregnated filter paper was studied as a screening test for galactosemia in the newborn. A 3-mm disc punched from blood-impregnated filter paper card was fixed with acetone-methanol and incubated in a reaction mixture containing galactose dehydrogenase and alkaline phosphatase. This reaction mixture was then spotted on DEAE-cellulose paper, dried, and observed under a UV-lamp. The minimum amount of galactose detected by this procedure was 2 mg/dl. Estimation of galactose and galactose-1-phosphate with this procedure correlated well with estimation by bacterial assay.

Escherichia coli↗
PubMedDate not supplied

Polyol pathway activity in nervous tissues of diabetic and galactose-fed rats: effect of dietary galactose withdrawal or tolrestat intervention therapy.

Enhanced polyol pathway activity resulting in an accumulation of sorbitol and a depletion of myoinositol in nervous tissues has been proposed to be important in development of diabetic neuropathies. This investigation demonstrated that in two models of diabetic complications, streptozocin (STZ)-induced diabetic rats and galactose-fed rats, 5 weeks of disease led to an accumulation of sorbitol or galactitol, respectively, in three cranial nerves (the optic (II), trigeminal (V), and vagus (X) nerves), as well as the sciatic nerve, cerebral cortex, and retina. In both models, the cranial nerves and cerebral cortex contained lower levels of accumulated polyol than the sciatic nerve. In addition, myoinositol depletion was observed in the sciatic nerve only. In a second galactose-fed rat study, returning 5-week galactose-fed rats to a normal diet for 6 weeks led to complete elimination of galactitol from the optic nerve, sciatic nerve, and retina and normalization of the sciatic nerve myoinositol concentration. Similarly, continuing the galactose diet for 6 more weeks (ie, a total of 11 weeks) as well as administration of the aldose reductase inhibitor (ARI) tolrestat (20 and 40 mg/kg/day), caused the sciatic nerve to contain a normal myoinositol concentration and a galactitol concentration that was 95% below the level observed in galactose-fed controls. In the optic nerve and retina, tolrestat was less effective, resulting in 69-78% lower galactitol levels. In conclusion, these findings indicate that sorbitol and galactitol accumulate in cranial nerves, brain, and retina without a concomitant decrease in myoinositol. Either withdrawal of the galactose diet or intervention with tolrestat normalized polyol levels in the sciatic nerve.(ABSTRACT TRUNCATED AT 250 WORDS)

Aldehyde Reductase↗
PubMed1997

Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site.

Galactose-1-phosphate uridylyltransferase plays a key role in galactose metabolism by catalyzing the transfer of a uridine 5'-phosphoryl group from UDP-glucose to galactose 1-phosphate. The enzyme from Escherichia coli is composed of two identical subunits. The structures of the enzyme/UDP-glucose and UDP-galactose complexes, in which the catalytic nucleophile His 166 has been replaced with a glycine residue, have been determined and refined to 1.8 A resolution by single crystal X-ray diffraction analysis. Crystals employed in the investigation belonged to the space group P2(1) with unit cell dimensions of a = 68 A, b = 58 A, c = 189 A, and beta = 100 degrees and two dimers in the asymmetric unit. The models for these enzyme/substrate complexes have demonstrated that the active site of the uridylyltransferase is formed by amino acid residues contributed from both subunits in the dimer. Those amino acid residues critically involved in sugar binding include Asn 153 and Gly 159 from the first subunit and Lys 311, Phe 312, Val 314, Tyr 316, Glu 317, and Gln 323 from the second subunit. The uridylyltransferase is able to accommodate both UDP-galactose and UDP-glucose substrates by simple movements of the side chains of Glu 317 and Gln 323 and by a change in the backbone dihedral angles of Val 314. The removal of the imidazole group at position 166 results in little structural perturbation of the polypeptide chain backbone when compared to the previously determined structure for the wild-type enzyme. Instead, the cavity created by the mutation is partially compensated for by the presence of a potassium ion and its accompanying coordination sphere. As such, the mutant protein structures presented here represent valid models for understanding substrate recognition and binding in the native galactose-1-phosphate uridylyltransferase.

Binding Sites↗
PubMed1977

2-Deoxy-D-galactose, a substrate for the galactose-transport system of Escherichia coli.

The following observations showed that 2-deoxy-D-galactose is a useful tool for the isolation and elucidation of the activity of one system for galactose uptake into Escherichia coli. 1. 2-Deoxygalactose, which is not a substrate for growth of E. coli, was transported into strains of the organism induced for galactose transport. 2. By using appropriate mutants it was shown that 2-deoxygalactose is a much better substrate for the galactose-transport system than for the methyl galactoside-transport system. This was confirmed by the results of mutual inhibition studies with substrates of each transport system. 3. The glucose-, arabinose- or lactose-transport systems did not effect significant transport of 2-deoxygalactose. 4. Like other substrates of the galactose-transport system, 2-deoxygalactose promoted effective proton uptake into de-energized suspensions of appropriate E. coli strains. 5. The S183 series of E. coli mutants were found to contain a constitutive galactose-transport system, if 2-deoxygalactose transport is used as one criterion for such activity.

Arabinose↗
PubMed1977

Effect on pancreatic blood flow and insulin output of infusions of aminophylline, galactose and galactose plus aminophylline into an isolated in situ portion of pancreas.

Effects on pancreatic blood flow and insulin output of infusions of aminophylline, galactose and galactose plus aminophylline were studied on an isolated portion of dog pancreas with only one afferent and one efferent blood vessel remaining. Infusion of aminophylline at 8 mg per minute gave significant increases in pancreatic blood flow and insulin output. Infusion of galactose at 7.2 mg per minute significantly increased insulin output. Galactose (7.2 mg per minute) plus aminophylline (8 mg per minute) also increased both pancreatic blood flow and insulin output. Pancreatic venous plasma glucose levels rose slightly during these infusions. Since the perfusing plasma contained a fasting level of glucose both aminophylling and galactose when infused alone or together were infused in the presence of approximately 1 mg/ml glucose. Pancreatic blood flow and insulin output increased to a lesser extent when aminophylline was infused along with galactose, the when aminophylline was infused alone.

Aminophylline↗
PubMed1985

Digestion and absorption rates of lactose, glucose, galactose, and fructose in three infants with congenital glucose-galactose malabsorption: perfusion studies.

The digestion rates of lactose and the absorption rates of glucose, galactose, and fructose were studied by continuous perfusion of the jejunum in three patients aged 7 weeks to 9 months with congenital glucose-galactose malabsorption (infusion rate:1.0 ml min-1; concentration of each sugar: 200 mM; perfusion distance: 30 cm). The mean absorption rates of glucose and galactose were 26.5 and 43.8 mumol min-1 30 cm-1, respectively, and were significantly reduced (p less than 0.001) to 13 and 22%, respectively, of intake. On the other hand, the absorption of fructose was 133.3 mumol min-1 30 cm-1, i.e., as high as in the controls. The hydrolysis rate of lactose was also normal (134.0 mumol min-1 30 cm-1). However, the absorption rates of glucose and galactose released from the disaccharide were as low as the perfusion of free monosaccharides. In patients with glucose-galactose malabsorption the glucose absorption rate is as low as that of galactose. No additional glucose transport system seems to exist. A hydrolase related transport system is also of no importance in compensating for the primary defect of monosaccharide absorption.

Biological Transport, Active↗
PubMed1988

Lectin-carbohydrate interactions. Studies of the nature of hydrogen bonding between D-galactose and certain D-galactose-specific lectins, and between D-mannose and concanavalin A.

The binding of galactose-specific lectins from Erythrina indica (EIL), Erythrina arborescens (EAL), Ricinus communis (agglutinin; RCA-I), Abrus precatorius (agglutinin; APA), and Bandeiraea simplicifolia (lectin I; BSL-I) to fluoro-, deoxy-, and thiogalactoses were studied in order to determine the strength of hydrogen bonds between the hydroxyl groups of galactose and the binding sites of the proteins. The results have allowed insight into the nature of the donor/acceptor groups in the lectins that are involved in hydrogen bonding with the sugar. The data indicate that the C-2 hydroxyl group of galactose is involved in weak interactions as a hydrogen-bond acceptor with uncharged groups of EIL and EAL. With RCA-I, the C-2 hydroxyl group forms two weak hydrogen bonds in the capacity of a hydrogen-bond acceptor and a donor. On the other hand, there is a strong hydrogen bond between the C-2 hydroxyl group of galactose, which acts as a donor, and a charged group on BSL-I. The C-2 hydroxyl group of the sugar is also a hydrogen-bond donor to APA. The lectins are involved in strong hydrogen bonds through charged groups with the C-3 and C-4 hydroxyl groups of galactose, with the latter serving as hydrogen-bond donors. The C-6 hydroxyl group of the sugar is weakly hydrogen bonded with neutral groups of EIL, EAL, and APA. With BSL-I, however, a strong hydrogen bond is formed at this position with a charged group of the lectin. The C-6 hydroxyl groups is a hydrogen-bond acceptor for EIL and EAL, a hydrogen-bond donor for APA and BSL-I, and appears not to be involved in binding to RCA-I. The data with the thiosugars indicate the involvement of the C-1 hydroxyl group of galactose in binding to EIL, EAL, and BSL-I, but not to RCA-I and APA. We have also performed a similar analysis of the binding data of fluoro- and deoxysugars to concanavalin A [Poretz, R. D. and Goldstein, I. J. (1970) Biochemistry 9, 2890-2896]. This has allowed comparison of the donor/acceptor properties and free energies of hydrogen bonding of the hydroxyl groups of methyl alpha-D-mannopyranoside to concanavalin A with the results in the present study. On the basis of this analysis, new assignments are suggested for amino acid residues of concanavalin A [corrected] that may be involved in hydrogen bonding to the sugar.

Concanavalin A↗
PubMed1996

Isolation and structures of glycoprotein-derived free oligosaccharides from the unfertilized eggs of Scyliorhinus caniculus. Characterization of the sequences galactose(alpha 1-4)galactose(beta 1-3)-N-acetylglucosamine and N-acetylneuraminic acid(alpha 2-6)galactose(beta 1-3)-N-acetylglucosamine.

As previously reported [Ishii, K., Iwasaki, M., Inoue, S., Kenny, P. T. M., Komura, H. & Inoue, Y. (1989) J. Biol. Chem. 264, 1623-1630; Inoue, S., Iwasaki, M., Ishii, K., Kitajima, K. & Inoue, Y. (1989) J. Biol. Chem. 264, 18520-185261, the unfertilized eggs of two different species of fresh-water fish, Plecoglossus altivelis and Tribodolon hakonensis, contain relatively large amounts of free sialooligosaccharides. These oligosaccharides were found to derive from glycophosphoproteins, owing to the activity of a peptide - N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase [Iwasaki, M., Seko, A., Kitajima, K., Inoue, Y. & Inoue, S. (1992) J. Biol. Chem. 267, 24287-24296; Seko, A., Kitajima, K., Inoue, Y. & Inoue, S. (1991) J. Biol. Chem. 266, 22110-22114]. Here we describe a new type of free oligosaccharides, isolated from unfertilized eggs of Scyliorhinus caniculus. From the structural analysis, based upon 1H-NMR spectroscopy, the following glycan units are proposed.[Formula: see text]

Animals↗
PubMed2006

Galactose oxidase action on galactose containing glycolipids--a fluorescence method.

Features that alter the glycolipid sugar headgroup accessibility at the membrane interface have been studied in bilayer lipid model vesicles using a fluorescence technique with the enzyme galactose oxidase. The effects on oxidation caused by variation in the hydrophobic moiety of galactosylceramide or the membrane environment for galactosylceramide, monogalactosyldiacylglycerol and digalactosyldiacylglycerol were studied. For this study we combined the galactose oxidase method for determining the oxidizability of galactose containing glycolipids, and the fluorescence method for determining enzymatic hydrogen peroxide production. Exposed galactose residues with a free hydroxymethyl group at position 6 in the headgroup of glycolipids were oxidized with galactose oxidase and subsequently the resultant hydrogen peroxide was determined by a combination of horseradish peroxidase and 10-acetyl-3,7-dihydroxyphenoxazine (Amplex Red). Amplex Red reacts with hydrogen peroxide in the presence of horseradish peroxidase with a 1:1 stoichiometry to form resorufin. With this coupled enzyme approach it is also possible to determine the galactolipid transbilayer membrane distribution (inside-outside) in bilayer vesicles.

Fluorescence↗
PubMed1986

Microassay for estimation of galactose and galactose-1-phosphate in dried blood specimens.

A fluorometric assay for blood galactose and galactose-1-phosphate has been modified and improved to shorten the analysis time and to increase sensitivity above other published methods. The method may be useful as a quantitative screening or routine clinical test to detect infants suspected of having a defect of galactose metabolism. It can also be used to monitor blood galactose or galactose-1-phosphate levels in children with galactosemia who are on a lactose-free diet.

Alkaline Phosphatase↗
PubMed1983

Light microscopic histochemical detection of terminal galactose and N-acetylgalactosamine residues in rodent complex carbohydrates using a galactose oxidase--Schiff sequence and peanut lectin--horseradish peroxidase conjugate.

A technique was investigated for the direct visualization on paraffin sections of galactose and N-acetylgalactosamine residues terminating saccharide chains in complex carbohydrates. Sections were incubated with the enzyme galactose oxidase (GO), which oxidizes the C-6 hydroxyl of galactose or N-acetylgalactosamine (GalNAc) residues, and the resulting aldehyde was visualized by its reaction with Schiff's reagent. Submaxillary and sublingual glands, pancreas, stomach, duodenum, and ileum from mice and rats were stained with the GO-Schiff sequence and results were compared with staining by a peanut lectin-horseradish peroxidase (PL-HRP) conjugate that binds selectively to terminal galactose and preferentially to the terminal dimer beta-D-Gal-(1 leads to 3)-D-GalNAc. Three classes of reactive sites were revealed: 1) those reactive with both GO-Schiff and PL-HRP, 2) those stained with the GO-Schiff sequence but unreactive with PL-HRP, and 3) those GO-Schiff unreactive but PL-HRP positive. Based on the carbohydrate binding specificity of GO and PL, it is suggested that tissue complex carbohydrates in group one contain terminal beta-galactose residues with unmodified hydroxyls at C-2, C-4, and C-6, whereas those in group two contain terminal GalNAc residues. The structure of oligosaccharides in group 3 sites remains enigmatic.

Acetylgalactosamine↗
PubMed2007

Galactose oxidase immobilized on silica in an analytical determination of galactose-containing carbohydrates.

Galactose oxidase from Fusarium graminearum IMV-1060 adsorbed on, and covalently bound to, silica carriers has been used for analytical determinations of D-galactose and galactose-containing sugars. Using a flowing oxygen electrode of the Clark-type, sensor system for enzymatic analysis of water solutions of galactose-containing carbohydrates was made. Measurements were taken both in the pulse and continuous modes of a substrate flowing through a column with an immobilized biocatalyst. The linear measurement ranges for galactose-containing carbohydrates concentrations were determined.

Adsorption↗
PubMed1995

Determination of galactose in human blood by high-performance liquid chromatography: comparison with an enzymatic method and application to the pharmacokinetic study of galactose in patients with liver dysfunction.

Galactose, the C-4 epimer of glucose, is an agent of choice for the quantitation of liver function. A simple, precise, and accurate high-performance liquid chromatographic (HPLC) assay with refractive index detection was developed for the determination of galactose in human whole blood. The method consists of organic solvent-heavy metal deproteinization procedures and reversed-phase chromatography on a cation-exchange column in the calcium form. Calibration graphs were linear over the concentration range 100-2500 microgram/mL, with correlation coefficients > 0.999. The within-day coefficient of variation (CV) ranged from 2.08 to 8.94%, and the between-day CV ranged from 1.61 to 10.9%. The limit of quantitation was 100 micrograms/mL in whole blood. However, the limit of detection was 75 micrograms/mL based on a signal-to-noise ratio of > or = 3. Eight structurally related sugars and polyols were investigated to check for potential interferences using the analytical condition of the assay. The possible metabolites of galactose present in the body were also checked to determine the specificity of this assay. The proposed HPLC assay was compared with an enzymatic assay and an excellent correlation was observed (HPLC = 1.0299Enz. - 12.907, r = 0.952, p < 0.001). This HPLC method has been successfully applied to the pharmacokinetic study of galactose in six patients with liver dysfunction. Following the intravenous administration of a dose of 0.5 g/kg body weight, galactose pharmacokinetics followed a nonlinear two-compartment model with Michaelis-Menten elimination from the central compartment.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1995

In vivo oxidation of [13C]galactose in patients with galactose-1-phosphate uridyltransferase deficiency.

We developed an intravenous and oral [13C]galactose breath test for the in vivo study of galactose metabolism. Following an intravenous bolus of 7 mg/kg of [1-13C]galactose in the fasting state, normal children and adults eliminated 3-6% and 21-47% of the bolus as 13CO2 in expired air collected over 1 and 5 h, respectively. Comparable fractional elimination was seen when the dose was given orally. Patients with galactosemia who have barely detectable or absent galactose-1-phosphate uridyltransferase (GALT) activity in erythrocytes and are homoallelic for the Q188R gene mutation, when given a 7 mg/kg intravenous bolus had barely detectable 13CO2 in air samples in the first hour, but eventually eliminated as much as 3.6% of the dose in 5 h. A galactosemia/Duarte (Q188R/N314D) compound heterozygote and a homozygous Duarte subject, as well as a subject with one normal allele and one Q188R allele, showed normal in vivo oxidation. An assessment of whole body galactose metabolism can be made with this procedure. Further use of this in vivo modality in patients with different genetic backgrounds should increase our understanding of genotype-phenotype relationships in hereditary galactosemia.

Adolescent↗
PubMed1986

Oral intake of glucose plus galactose and erythrocyte galactose-1-phosphate. A nutritional evaluation of hydrolyzed lactose.

This study deals with the metabolic effects of hydrolyzed lactose: After an overnight fast 5 healthy adult volunteers consumed a glucose-galactose mixture equivalent to 61.4 g of lactose (or 125 g of a dried skim milk powder with hydrolyzed lactose). The postprandial rise of erythrocyte galactose-1-phosphate (gal-1-P) never exceeded 22.3 mumol per liter packed red blood cells. This amounts to no more than 22% of the levels known from galactosemic children to be safe, concerning ocular, neural or hepatic damage. We conclude that the consumption of the hydrolyzed lactose does not cause a risk for consumer's health as judged from this galactose metabolite. A considerably higher risk, however, may accompany the consumption of galactose alone which causes around 17-fold higher plasma galactose levels and around 8-fold higher erythrocyte gal-1-P concentrations for more extended time periods.

Adult↗