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PubMedDate not supplied

Metabolism of pirprofen in man, monkey, rat, and mouse.

Pirprofen was well absorbed by man, rhesus monkey, rat, and mouse after oral administration of a solution of 14C-labeled compound. The major route of elimination of radioactivity in all four species was renal, mostly in the form of metabolites. Twelve metabolites of pirprofen, accounting for 80% or more of the urinary radioactivity, were identified in the urine of the four species. The metabolic pathways of pirprofen involved oxidation to the pyrrole analogue, and oxidation of the pyrroline double bond to an epoxide, followed by opening of the oxirane ring to a trans-diol derivative. Scission of the pyrroline or pyrrole ring was also observed, leading to the corresponding aniline-type metabolite, part of which underwent subsequent acetylation. Conjugation of the propionic acid functionality with glucuronic acid was found to be extensive in the mouse, rhesus monkey, and man, but not in the rat. Conjugation with taurine was also observed in the rat and mouse.

Adult↗
PubMed1983

Glycosyl acceptors in intact and permeabilized normal and cystic fibrosis fibroblasts.

Using cell permeabilization, a technique which allows addition of exogenously supplied radiolabeled sugar nucleotides to serve as direct glycosyl donors, oligosaccharide biosynthesis was examined in fibroblasts obtained from normal and cystic fibrosis (CF) subjects. Incubation of logarithmically growing cells with either radiolabeled leucine or xylose has indicated that there was a difference in the synthetic rate between the cell types. Protein synthesis in normal cells made permeable with 50 micrograms/ml lysolecithin (LL) was demonstrated to be absent, and could not be induced to take place by adding exogenous components, including energy sources and amino acids, normally required for protein synthesis. Thus radiolabeled sugars were being added to peptide acceptors which were already present at the time of LL addition. Both permeable and intact fibroblasts were exposed to labeled UDP-xylose, UDP-galactose, and UDP-glucuronic acid, all donors of mucopolysaccharide precursors. The uptake of xylose into protein was the same for both normal and CF cells, but permeable CF fibroblasts incorporated statistically greater amounts of sugar from UDP-galactose and UDP-glucuronic acid. Intact CF cells were also labeled using these two sugar nucleotides. Trypan blue exclusion indicated CF and normal fibroblasts were equally intact. This and the fact that preincubation of CF cells with the appropriate cold sugar nucleotide eliminated the differences in incorporation between the normal and CF cells suggested that CF fibroblasts had more cell surface acceptor than the normal cells.

Biological Transport↗
PubMed1990

Acyl glucuronidation and glucosidation of pranoprofen, a 2-arylpropionic acid derivative, in mouse liver and kidney homogenates.

The formation of acyl glucuronide and glucoside of 2-(5H-[1]benzopyrano[2,3-b]pyridin-7-yl)propionic acid (pranoprofen), an anti-inflammatory drug, was studied in homogenates and microsomes of mouse tissues by using S(+)-, R(-)- and RS(+/-)-pranoprofen. Acyl glucuronidation occurred mainly in the liver, whereas acyl glucosidation was predominant in the kidney. Furthermore, both conjugations occurred by enzymatic transfer of glucuronic acid of uridine diphosphate glucuronic acid (UDPGA) and glucose of uridine diphosphate glucose (UDPG) to pranoprofen, respectively. No conjugation reactions were observed in the lung, plasma or gut. The amount of conjugates in the liver and kidney increased by the prolongation of the incubation times and reached the maximum at 15-30 min for glucuronidation and 45 min for glucosidation. After that, both conjugates decreased with the lapse of time. Both acyl conjugates were the least stable in the liver, then in the kidney and the most stable in the plasma. In the liver, acyl glucoside was converted to acyl glucuronide and pranoprofen in the presence of UDPGA, but only a small amount of acyl glucuronide was changed to acyl glucoside in the kidney in spite of the presence of UDPG. In the kidney, acyl glucoside decreased relative to acyl glucuronide at increasing doses for both S(+)- and R(-)-pranoprofen, but the concentration of acyl glucoside was much higher for S(+)-pranoprofen than R(-)-enantiomer 1 h after the oral administration of S(+)- and R(-)-pranoprofen. No acyl glucoside was detected in the liver and plasma. Although only a small difference in acyl glucuronidation in the liver was observed between S(+)- and R(-)-enantiomers, acyl glucosidation in the kidney occurred more predominantly for S(+)-pranoprofen than for the R(-)-enantiomer.

Animals↗
PubMed1985

Effect of anti-inflammatory drugs on xanthine oxidase and xanthine oxidase induced depolymerization of hyaluronic acid.

The inhibitory effect of various anti-inflammatory drugs on the xanthine oxidase derived depolymerization of hyaluronic acid was studied. The depolymerization was assayed by repeated viscosity measurements. By using a low xanthine oxidase activity, the decrease in viscosity with time followed first order reaction kinetics and was therefore suitable for kinetic analysis. The xanthine oxidase activity was monitored by assay of O2-consumption with a Clark-electrode and by assay of urate production. We present evidence that salicylic, acetylsalicylic, gentisic and azodisalicylic acid and sulfasalazine inhibit the production of oxygen-derived free radicals by xanthine oxidase. We found that sulfapyridine, 5-aminosalicylic acid, allopurinol, mannitol, glucuronic acid and N-acetylglucosamine in addition to the earlier studied drugs, paracetamol, ibuprofen, benoxaprofen and gentisic acid exert their effect via scavenging of free radicals. These drugs had very little effect on the enzyme activity.

Anti-Inflammatory Agents↗
PubMedDate not supplied

Identification of detomidine carboxylic acid as the major urinary metabolite of detomidine in the horse.

Horse urine was investigated for metabolites by chromatography and mass spectrometry following the oral administration of the large animal analgesic sedative detomidine to two stallions and intravenous administration of [3H]-detomidine to a mare. Detomidine carboxylic acid and hydroxydetomidine glucuronic acid conjugate were identified in the urine after the oral doses. In addition, traces of free hydroxydetomidine were observed. About half of the radioactivity of [3H]-detomidine was excreted in the urine in 12 h after the i.v. dose (80 micrograms/kg). Most of the excretion occurred between 5 and 12 h in contrast to urine output which was highest 2-5 h after the dosing. The major radioactive metabolite in the urine was detomidine carboxylic acid. It comprised more than two thirds of the total metabolites in all the urine fractions collected. Its excretion profile was similar to that of total radioactivity. Hydroxydetomidine glucuronide was also excreted. It contributed 10-20% of the total metabolites in the urine. The free aglycone was only seen in the samples collected during the peak urine flow. A minor metabolite was tentatively characterized as the glucuronide of N-hydroxydetomidine.

Analgesics↗
PubMed2005

Biosynthesis of UDP-xylose: characterization of membrane-bound AtUxs2.

UDP-xylose (UDP-Xyl) is a sugar donor for the synthesis of glycoproteins, polysaccharides, various metabolites, and oligosaccharides in plants, vertebrates, and fungi. In plants, the biosynthesis of UDP-Xyl from UDP-glucuronic acid (UDP-GlcA) appears to be catalyzed by numerous UDP-glucuronic acid decarboxylase (Uxs) isoforms. For example, six Uxs isoforms in Arabidopsis thaliana (L.) and four in rice have been identified. However, the reason/s for the existence of several isoforms that are necessary for the synthesis of UDP-Xyl remains unknown. Here, we describe a Uxs isoform in Arabidopsis, AtUXS2, encoding an integral membrane protein that appears to be localized to the Golgi apparatus. The enzyme is a dimer and has distinct properties. Unlike the UXS3 isoform, which is shown here to be a soluble protein, the UXS2 isoform is membrane bound. The characteristics of the membrane-bound AtUxs2 and cytosolic AtUxs3 support the hypothesis that unique UDP-GlcA-DCs possessing distinct sub-cellular localizations can spatially regulate specific xylosylation events in plant cells.

Arabidopsis↗
PubMed1987

Stimulation of human peripheral lymphocytes and induction of interleukin 2 production by a lectin from the gonad of the sea hare, Aplysia fasciata.

The lectin from gonads of the sea hare, Aplysia fasciata, which reacts with D-galacturonic acid and D-galactose derivatives, was purified by affinity chromatography on Sepharose 4B. The purified lectin was shown to stimulate human peripheral blood lymphocytes and to induce interleukin 2 production like PHA. These activities were specifically inhibited by D-galactose and neutralized galacturonic acid (not by glucuronic acid). The rate of lymphocyte proliferation was similar at 72 and 96 hours in culture. The main stimulation was observed in the T lymphocyte population obtained by rosette formation with sheep red blood cells.

Animals↗
PubMed1982

Further characterization of the antithrombin-binding sequence in heparin.

An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin and previously found to have the following predominant structure (see formula in text) has been studied further. High-voltage, paper electrophoresis of the 3H-labelled disaccharides obtained by deamination with HNO2 (pH 1.5) followed by reduction with Na[3H]BH4 showed approximately 25% of mono-O-sulfated components, in addition to L-iduronic acid(2-O-SO3)-2,5-anhydro-D-[3H]mannitol (6-O-SO3). The monosulfated disaccharides were identified by high pressure, ion-exchange chromatography as L-iduronic acid(2-O-SO3)-2,5-anhydro-D-[3H]mannitol, L-Iduronic acid-2,5-anhydro-D-[3H]mannitol(6-O-SO3). and D-glucuronic acid-2,5-anhydro-D-[3H]-mannitol L, iduronic acid 2,5-anhydro-D-[3H]mannitol(6-O-SO3), and D-glucuronic acid-2,5-anhydro-D-[3H]-mannitol. These components originated from the reducing, terminal disaccharide residue (units 7 and 8), as indicated by selective labelling with Na[3H]-BH4. The structural variability within this region suggests that it is not part of the antithrombin-binding sequence. Neither enzymic removal of the non-sulfated L-iduronic acid unit 1 nor N-deacetylation (by hydrazinolysis) at unit 2 had any significant effect on the affinity of the octasaccharide for antithrombin. However, removal of the disaccharide corresponding to units 1 and 2, by selective deamination of the N-deacetylated octasaccharide, yielded a low-affinity hexasaccharide. In addition, a high-affinity deamination product was formed, presumably an octasaccharide containing a 6-sulfated 2-deoxy-2-C-formyl-D-pentofuranosyl unit due to ring contraction in unit 2. These results suggest that the 6-sulfate group in unit 2 may be involved in antithrombin binding. It is concluded that the antithrombin binding site in heparin is represented by the pentasaccharide sequence extending from unit 2 to unit 6 of the octasaccharide studied.

Animals↗
PubMed1997

Quantitative analysis of neutral and acidic sugars in whole bacterial cell hydrolysates using high-performance anion-exchange liquid chromatography-electrospray ionization tandem mass spectrometry.

A procedure for analysis of a mixture of neutral and acidic sugars in bacterial whole cell hydrolysates using high-performance anion-exchange liquid chromatography-electrospray ionization tandem mass spectrometry (HPAEC-ESI-MS-MS) is described. Certain bacteria (including bacilli), grown under phosphate-limited conditions, switch from producing a teichoic acid (containing ribitol) to a teichuronic acid (characterized by glucuronic acid content). Bacterial cells were hydrolyzed with sulfuric acid to release sugar monomers. The solution was neutralized by extraction with an organic base. Hydrophobic and cationic contaminants (including amino acids) were removed using C18 and SCX columns, respectively. HPAEC is well established as a high-resolution chromatographic technique, in conjunction with a pulsed amperometric detector. Alternatively, for more selective detection, sugars (as M-H- ions) were monitored using ESI-MS. In HPAEC, the mobile phase contains sodium hydroxide and sodium acetate, which are necessary for chromatographic separation of mixtures of neutral and acidic sugars. Elimination of this high ionic content prior to entry into the ESI ion source is vital to avoid compromising sensitivity. This was accomplished using an on-line suppressor and decreasing post-column flow-rates from 1 ml to 50 microliters/min. In the selected ion monitoring mode, background (from the complex sample matrix as well as the mobile phase) was eliminated, simplifying chromatograms. Sugar identification was achieved by MS-MS using collision-induced dissociation.

Bacillus subtilis↗
PubMed1999

Isolation and analysis of a novel acidic polysaccharide from the case of squid pen.

A new non-sulphated acidic polysaccharide with an average molecular mass of 55 kDa was isolated from squid pen case after papain digestion and beta-elimination. This polysaccharide contains mainly L-iduronic acid, D-glucuronic acid, D-galactosamine, D-glucosamine and significant amounts of neutral sugars as glucose, galactose and fucose. The polysaccharide was not degraded to the relative disaccharides by chondroitinases ABC, AC and B, hyaluronidase and keratanase or by treatment with heparinases, suggesting a structure different from those of known glycosaminoglycans. The polysaccharide cannot form self aggregates.

Animals↗
PubMed2003

Analysis of reducing carbohydrates by reductive tryptamine derivatization prior to micellar electrokinetic capillary chromatography.

A micellar electrokinetic capillary chromatography method for determination of low molecular weight carbohydrates (dp 1-2) with an unbound carbonyl group as in aldoses or other reducing carbohydrates has been developed. Reductive amination of aldoses on the carbonyl group using tryptamine introduced a chromophor system to the carbohydrates enabling their sensitive UV detection at 220 nm and identification based on the indole group using diode array detection. Twelve carbohydrates including pentoses (d-ribose, l-arabinose, and d-xylose), hexoses (d-glucose, d-mannose, and d-galactose), deoxy sugars (l-rhamnose and l-fucose), uronic acids (d-glucuronic acid and d-galacturonic acid), and disaccharides (cellobiose and melibiose) are included in the study, using d-thyminose (2-deoxy-d-ribose) as the internal standard. Detection of all 12 carbohydrates is performed within 30 min. Linearity with correlation coefficients from 0.9864 to 0.9992 was found in the concentration range of 25-2500 micromol/L for all carbohydrates; the relative standard deviation on the migration times was between 0.27 and 0.80 min, and limits of quantification and limits of determination were in the picomole range.

Carbohydrates↗
PubMed1980

The acid lability of the glycosidic bonds of L-iduronic acid residues in glycosaminoglycans.

Heparan sulphate, heparin and dermatan sulphate were hydrolysed in 0.5M-H2SO4 at 100 degrees C. At intervals portions of the hydrolysate were removed and treated with HNO2 at pH 4.0 to cleave the glycosidic bonds of the N-unsubstituted hexosamine residues and to convert both free and combined hexosamines into anhydrohexoses. These hydrolysis/deamination mixtures were reduced with NaB3H4 and analysed by radiochromatography for alpha-L-iduronosylanhydrohexose, beta-D-glucuronosylanhydrohexose, and the free uronic acids and anhydrohexose. These data gave a kinetic profile of the cleavage of the alpha-L-iduronosyl and the beta-D-glucuronosyl bonds in these glycosaminoglycans. The beta-D-glucuronosyl bonds showed the expected resistance to acid hydrolysis, but the alpha-L-iduronosyl bonds were found to be as labile to acid as some neutral sugar glycosides. This unusual lability of alpha-D-iduronosyl-anhydromannitol and beta-D-glucuronosylanhydromannitol. The procedures used to follow the kinetics of glycosaminoglycan hydrolysis can also be sued to obtain quantitative analyses of L-iduronic acid, D-glucuronic acid and hexosamine in these polymers.

Chemical Phenomena↗
PubMed1995

Structure determination of the octa- and decasaccharide sequences isolated from the carbohydrate-protein linkage region of porcine intestinal heparin.

Previously we isolated a tetrasaccharide-serine and a hexasaccharide-serine from the carbohydrate-protein linkage region of porcine intestinal heparin after digestion with a mixture of Flavobacterium heparinase and heparitinases I and II (Sugahara, K., Yamada, S., Yoshida, K., de Waard, P., and Vliegenthart, J.F.G. (1992) J. Biol. Chem. 267, 1528-1533). In this study four longer carbohydrate sequences (I-IV) attached to Ser or a dipeptide (Ser-Gly or Gly-Ser), which accounted for at least 18.2% of the total linkage region, were isolated from the same heparin preparation after digestion with heparinase only. IV was successfully isolated only after subsequent digestion with glycuronate-2-sulfatase. Their structures were determined by chemical and enzymatic analyses and 1H NMR spectroscopy and found to be the following octa- and decasaccharide sequences attached to Ser in a molar ratio of 1.1:2.3:1.0:1.3: delta HexA(2S)alpha 1-4GlcN(NS,6S)alpha 1-4GlcA beta 1-4GlcNAc alpha 1-4- GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser (I), delta HexA(2S)alpha 1- 4GlcN(NS,6S)alpha 1-4IdoA alpha 1-4GlcNAc alpha 1-4GlcA beta 1- 3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser (II), delta HexA(2S)alpha 1- 4GlcN(NS,6S)alpha 1- 4IdoA alpha 1-4GlcNAc alpha 1-4GlcA beta 1-4GlcNAc-alpha 1- 4GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser (III), delta HexA alpha 1-4GlcN(NS,6S)alpha 1-4IdoA alpha 1-4GlcNAc(6S)alpha 1- 4GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser (IV) (delta HexA, GlcA, IdoA, and GlcN represent 4,5-unsaturated hexuronic acid, D-glucuronic acid, L-iduronic acid, and D-glucosamine, whereas 2S, 6S, and NS stand for 2-sulfate, 6-sulfate, and N-sulfate, respectively). I and II contained 1 mol of Gly in addition to Ser. The four structures indicate that sulfation in heparin chains takes place on the monosaccharide residues located in closer vicinity to the core protein than found for heparan sulfate chains and that there exist at least several heparin subclass chains with different linkage region structures. The significance of the isolated structures is discussed in relation to the biological functions and the biosynthetic mechanisms of heparin.

Amino Acids↗
PubMed1995

Enzymic reconstruction of glycosaminoglycan oligosaccharide chains using the transglycosylation reaction of bovine testicular hyaluronidase.

The reconstruction of glycosaminoglycan chains using the transglycosylation reaction of testicular hyaluronidase was investigated. First, the optimal conditions for the transglycosylation reaction catalyzed by the enzyme were determined by incubation with the enzyme, using hyaluronic acid (M(r) = 800,000) as a donor and pyridylaminated hyaluronic acid hexasaccharide having glucuronic acid at the nonreducing terminal as an acceptor. The carbohydrate chains as reaction products were determined by high performance liquid chromatography and mass spectrometry. The optimal pH for hydrolysis by the enzyme was found to be about 5.0, whereas that for the transglycosylation reaction was about 7.0. Sodium chloride in the reaction medium inhibited the transglycosylation reaction. Under the optimal conditions, the carbohydrate chains were sequentially transferred along with disaccharide units to the nonreducing terminal of the acceptor and elongated up to docosasaccharide from the acceptor, pyridylaminated hexasaccharide. Using a combination of hyaluronic acid, chondroitin, and chondroitin 4- and 6-sulfate as an acceptor and a donor, it was possible to reconstruct hybrid chains, which were natural or unnatural types of glycosaminoglycan chains. Therefore, it is highly likely that application of the transglycosylation reaction using testicular hyaluronidase would facilitate artificial reconstruction of glycosaminoglycans having some physiological functions.

Animals↗
PubMed2002

Transport of UDP-galactose in plants. Identification and functional characterization of AtUTr1, an Arabidopsis thaliana UDP-galactos/UDP-glucose transporter.

The synthesis of non-cellulosic polysaccharides and glycoproteins in the plant cell Golgi apparatus requires UDP-galactose as substrate. The topology of these reactions is not known, although the orientation of a plant galactosyltransferase involved in the biosynthesis of galactomannans in fenugreek is consistent with a requirement for UDP-galactose in the lumen of the Golgi cisternae. Here we provide evidence that sealed, right-side-out Golgi vesicles isolated from pea stems transport UDP-galactose into their lumen and transfer galactose, likely to polysaccharides and other acceptors. In addition, we identified and cloned AtUTr1, a gene from Arabidopsis thaliana that encodes a multitransmembrane hydrophobic protein similar to nucleotide sugar transporters. Northern analysis showed that AtUTr1 is indeed expressed in Arabidopsis. AtUTr1 is able to complement the phenotype of MDCK ricin-resistant cells; a mammalian cell line deficient in transport of UDP-galactose into the Golgi. In vitro assays using a Golgi-enriched vesicle fraction obtained from Saccharomyces cerevisiae expressing AtUTr1-MycHis is able to transport UDP-galactose but also UDP-glucose. AtUTr1- MycHis does not transport GDP-mannose, GDP-fucose, CMP-sialic acid, UDP-glucuronic acid, or UDP-xylose when expressed in S. cerevisiae. AtUTr1 is the first transporter described that is able to transport UDP-galactose and UDP-glucose. Thus AtUTr1 may play an important role in the synthesis of glycoconjugates in Arabidopsis that contain galactose and glucose.

Amino Acid Sequence↗
PubMed1998

Disaccharide analysis of heparin and heparan sulfate using deaminative cleavage with nitrous acid and subsequent labeling with paranitrophenyl hydrazine.

Compositional analyses of heparin (Hep) and heparan sulfate (HS) have been undertaken with disaccharide units obtained by either enzymatic digestion with heparitinases or hydrazinolysis/deamination reaction of polysaccharides. Unsaturated disaccharide units generated by the enzymatic method are detectable on HPLC with a uv detector recording absorbance at 230 nm. On the other hand, disaccharide units generated by the chemical method possess a component of 2,5-anhydromannose (AnMan) bearing aldehyde groups in addition to intact iduronic acid (IdoA) or glucuronic acid (GlcA). The aldehyde groups of the disaccharide units are usually reduced with sodium borotritide, and detected by radiochromatography. Both of them, however, involve inevitable experimental problems, such as the use of costly enzymes and radioisotopes. In the present study, we have established a novel composition analysis system for Hep and HS essentially based on the chemical method. After hydrazinolysis/deamination treatment of Hep and HS, the aldehyde groups of AnMan in the disaccharide units generated were coupled with paranitrophenyl (PNP-) hydrazine instead of reduction with sodium borotritide, AnMan-CH=N-NH-PNP (AnMan-PNP) being formed. Then, the PNP-labeled disaccharides were pre-treated on a SepPak C-18 cartridge column, and subsequently separated and detected on ion-pairing reversed-phase HPLC with a detector recording absorbance at 390 nm. With the present system, the order of elution was GlcA-AnMan-PNP (GM), IdoA-AnMan-PNP (IM), IdoA(2S)-AnMan-PNP (ISM), IdoA-AnMan(6S)-PNP (IMS), and IdoA(2S)-AnMan(6S)-PNP (ISMS). As an application, the disaccharide compositions of heparin from bovine intestine and heparan sulfate from bovine kidney were analyzed by the present method, and the results were comparable to those obtained by a well-established enzymatic method. The present compositional analysis was demonstrated to be reliable and economical.

Acetylation↗
PubMed2001

Comparison of cell-wall polysaccharides from Nectria cinnabarina with those from the group of Nectria with Sesquicillium anamorphs.

Alkali-extractable and water-soluble polysaccharides were purified from cell walls of five species of Sesquicillium or its teleomorphs, Nectria lasiacidis and Nectria impariphialis, and from Nectria cinnabarina, the type species of Nectria, a heterogeneous genus that belongs to the Hypocreales. Methylation and NMR analyses for determination of linkage types and structure were performed and indicated differences between the polysaccharides purified during the present study and those isolated from other nectrioid fungi, namely the presence of 5-O-substituted galactofuranose (-->5)-Galf-(1-->) in the main chain together with 2,6-di-O-substituted galactofuranose (-->2,6)-Galf-(1-->) residues in Sesquicillium buxi and Sesquicillium pseudosetosum. The polysaccharide from N. impariphialis was similar to those obtained from the above species, although an additional residue of 6-O-substituted glucopyranose (-->6)-Glcp-(1-->), was detected in some side chains. In N. lasiacidis and Sesquicillium candelabrum the polysaccharide contained an additional branching point of 5,6-di-O-substituted galactofuranose (-->5,6)-Galf-(1-->) linked to terminal N-acetylglucosamine GlcNAc-(1-->). These chains were linked to a small mannan core. All these polysaccharides showed major differences to the polysaccharide of N. cinnabarina, which was formed by a main chain of (1-->6)-beta-linked galactofuranose units almost fully branched at positions 2-O by either single residues of glucopyranose or acidic chains containing glucuronic acid and mannose.

Ascomycota↗
PubMed1989

Structural studies on the neutral polysaccharide of Bacillus subtilis AHU 1219 cell walls.

A neutral and an acidic polysaccharide with molecular masses of about 22 kDa and 45 kDa, respectively, were isolated from the N-acetylated cell walls of Bacillus subtilis AHU 1219 by heating at pH 2.5, followed by separation of the water-soluble product by ion-exchange chromatography and gel chromatography. The neutral polysaccharide, accounting for 40% of the mass of the cell walls, contained glucose, N-acetylglucosamine, N-acetylgalactosamine and N-acetylmannosamine in a molar ratio of 1:2:1:1. The minor, acidic polysaccharide contained glucuronic acid, glucose, galactose, L-serine and L-threonine in an approximate molar ratio of 1:1:1:0.5:0.5. Lysozyme digestion of the N-acetylated cell walls gave a polymer containing the neutral polysaccharide and glycopeptide components and another polymer which contained the acidic polysaccharide components together with small proportions of the neutral polysaccharide and glycopeptide components. Thus, the neutral and acidic polysaccharide chains seem to be attached to peptidoglycan through acid-labile linkages in the cell walls of this strain. Structural analysis of the neutral-polysaccharide preparation, involving 1H-NMR and 13C-NMR measurement, methylation and Smith degradation, led to the most likely structure, ----6)[Glc(beta 1----3)]GalNAc(alpha 1----4)-[GlcNAc(beta 1----3)]ManNAc(beta 1----4)GlcNAc(beta 1----, for the repeating units of this polysaccharide.

Amino Acids↗