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PubMed2000

Modeling reduction of uranium U(VI) under variable sulfate concentrations by sulfate-reducing bacteria.

The kinetics for the reduction of sulfate alone and for concurrent uranium [U(VI)] and sulfate reduction, by mixed and pure cultures of sulfate-reducing bacteria (SRB) at 21 +/- 3 degrees C were studied. The mixed culture contained the SRB Desulfovibrio vulgaris along with a Clostridium sp. determined via 16S ribosomal DNA analysis. The pure culture was Desulfovibrio desulfuricans (ATCC 7757). A zero-order model best fit the data for the reduction of sulfate from 0.1 to 10 mM. A lag time occurred below cell concentrations of 0.1 mg (dry weight) of cells/ml. For the mixed culture, average values for the maximum specific reaction rate, V(max), ranged from 2.4 +/- 0.2 micromol of sulfate/mg (dry weight) of SRB. h(-1)) at 0.25 mM sulfate to 5.0 +/- 1.1 micromol of sulfate/mg (dry weight) of SRB. h(-1) at 10 mM sulfate (average cell concentration, 0.52 mg [dry weight]/ml). For the pure culture, V(max) was 1.6 +/- 0.2 micromol of sulfate/mg (dry weight) of SRB. h(-1) at 1 mM sulfate (0.29 mg [dry weight] of cells/ml). When both electron acceptors were present, sulfate reduction remained zero order for both cultures, while uranium reduction was first order, with rate constants of 0.071 +/- 0.003 mg (dry weight) of cells/ml. min(-1) for the mixed culture and 0.137 +/- 0.016 mg (dry weight) of cells/ml. min(-1) (U(0) = 1 mM) for the D. desulfuricans culture. Both cultures exhibited a faster rate of uranium reduction in the presence of sulfate and no lag time until the onset of U reduction in contrast to U alone. This kinetics information can be used to design an SRB-dominated biotreatment scheme for the removal of U(VI) from an aqueous source.

Clostridium↗

PubMed1997

NMR spectroscopic analysis of sulfated beta-1,3-xylan and sulfation stereochemistry.

A novel sulfated beta-1,3-xylan product was synthesized from algal cell wall microfibril homoxylan by the N,N-dimethylformamide (DMF)-SO3 complex sulfation method. Antithrombin activity appeared in this product was 6.5 times higher than that of standard heparin. From the results of 1H- and 13C-NMR spectroscopic analyses by DQF-COSY and HMQC and an infrared spectroscopic analysis, it was revealed that the ordered structure of beta-1,3-xylan as a triple helix had decayed and the resulting conformational changes had been caused by the sulfation reaction. The sulfated positions on the C-4 hydroxyl groups of the xylose residues were determined from 13C-NMR chemical shifts, and it was found that regioselective sulfation had occurred predominantly with the C-4 secondary hydroxyl groups to produce a mono-substituent. Another type of sulfation of beta-1,4-xylan that showed no regioselectivity is considered to have been due to the different conformation of both xylans chains such as the triple helix in beta-1,3-xylan and the double straight chain like cellulose in beta-1,4-xylan. Therefore, the different type of regioselective sulfation of beta-1,3- and beta-1,4-xylan was caused by the difference in steric hindrance due to these conformations. These different types of regioselective sulfation with different linkage positions are also discussed for the secondary hydroxyl groups in beta-1,3- and beta-1,4-glucan after chemoselective sulfation of the C-6 primary hydroxyl groups.

Antithrombins↗

PubMed1985

N-sulfation of heparan sulfate with microsomal fraction of endometrium of rabbit uterus.

Heparan sulfate was prepared from the pronase digest of the porcine kidney and modified chemically to yield N-desulfated, N-, O-desulfated, and N- O-desulfated N-acetylated heparan sulfates. Heparan sulfate and its modifications thus obtained were used as substrates to measure the sulfotransferase activity in the microsomal fraction of the endometrium of the rabbit uterus. N-, O-Desulfated heparan sulfate was the best acceptor of sulfate from 3'-phosphoadenylyl [35S] sulfate and intact heparan sulfate was the poorest one. The products of enzymatic reaction were treated with nitrous acid and examined by gel-filtration and electrophoresis. The results indicated that sulfate was almost exclusively incorporated as N-sulfate into all the present substrates.

Animals↗

PubMed1975

The separation and identification of dopamine 3-O-sulfate and dopamine 4-O-sulfate in urine of Parkinsonian patients.

A method is described for the isolation and measurement of dopamine 3-O-sulfate and dopamine 4-O-sulfate. The sulfate isomers of dopamine were synthesized chemically by the reaction of dopamine with sulfuric acid. The isomers were isolated by anion-exchange column chromatography and the identities of the two isomers were confirmed by gas chromatography coupled with mass spectrometry. A method is described for the assay of the two isomers by high-pressure liquid chromatography. When Parkinsonian patients were treated with 4.0 g/day of L-dopa, the amount of dopamine 3-O-sulfate excreted in the urine was 19.6 times that of dopamine 4-O-sulfate. When untreated Parkinsonian patients received tracer quantities of 3H-L-dopa either intravenously or orally, 3H-dopamine 3-O-sulfate was the predominant isomer but the amounts were only 3 times those of the 4-isomer. Greater quantities of both isomers were excreted when 3H-L-dopa was given orally as compared to intravenous administration. Since dopamine 3-O-sulfate is the predominant sulfate isomer, it is concluded that sulfate conjugation of dopamine could possibly compete with 3-O-methylation in determining the resultant conjugated product.

Administration, Oral↗

PubMed1991

Coupling of N-deacetylation and N-sulfation in a Chinese hamster ovary cell mutant defective in heparan sulfate N-sulfotransferase.

The coordination of N-deacetylation and N-sulfation of heparan sulfate was examined in wild-type Chinese hamster ovary cells and mutant pgsE-606. This mutant expresses about 3-fold less N-sulfotransferase activity, which causes the proportion of N-sulfated GlcN residues in heparan sulfate to decline from 39 to 21% of total GlcN (Bame, K.J., and Esko, J.D. (1989) J. Biol. Chem. 264, 8059-8065). In this report, we show that microsomes from pgsE-606 cells have about twice the N-deacetylase activity found in microsomes from wild-type cells. However, N-deacetylation in vivo was actually depressed since heparan sulfate preparations from the mutant contained very few unsubstituted GlcN residues and 2-fold less N-sulfated GlcN residues. Treatment of mutant cells with chlorate, a general inhibitor of sulfation, depressed adenosine 3'-phosphate-5'-phosphosulfate pools more than 10-fold and further reduced the extent of N-sulfation from 21% to less than 6% of total GlcN. Unsubstituted GlcN residues accumulated under these conditions to the extent that N-sulfated residues declined. Thus, N-deacetylation remained depressed in the mutant in the presence of chlorate. These findings show that N-deacetylation is regulated in vivo and support the idea that the activity of N-deacetylase may be linked to N-sulfotransferase.

Acetylation↗

PubMed1986

Secretory granules of heparin-containing rat serosal mast cells also possess highly sulfated chondroitin sulfate proteoglycans.

Rat serosal mast cells, which synthesize only heparin proteoglycans as detected by intrinsic labeling with [35S]sulfate, were analyzed for the presence of intracellular chondroitin sulfate proteoglycans by chemical and immunochemical means. Rat serosal mast cells of greater than 99% purity were treated with Zwittergent 3-12 and 4 M guanidine HCl, and the extracted nonradiolabeled proteoglycans were purified by density gradient centrifugation. As assessed by quantification of the unsaturated disaccharides released from the proteoglycans by chondroitinase ABC treatment, 10(6) rat serosal mast cells contained 2.4-4.5 micrograms of chondroitin sulfate proteoglycans. Analysis of the chondroitinase ABC digests by high performance liquid chromatography revealed the unsaturated disaccharides delta Di-4S, delta Di-diSB, and delta Di-diSE which were derived from GlcA----GalNAc-4-SO4, iduronic acid-2-SO4----GalNAc-4-SO4, and GlcA----GalNAc-4,6-diSO4, respectively. The molar ratio of the monosulfated to disulfated disaccharides was approximately 2:1 with delta Di-diSE greater than delta Di-diSB. When analyzed with a mouse anti-chondroitin sulfate monoclonal antibody and fluorescein-labeled F(ab')2 goat anti-mouse IgG, approximately 91% of permeabilized and chondroitinase ABC-treated cells in the mast cell preparations exhibited intracellular fluorescence, and the pattern of staining indicated that the chondroitin sulfate molecules were located in the secretory granules. The specificity of the monoclonal antibody for the unsaturated double bond created by chondroitinase ABC treatment of the proteoglycan in situ was established by the absence of fluorescence when the chondroitinase ABC step was omitted or when heparinase digestion was substituted for chondroitinase ABC. Furthermore, the ability of the anti-chondroitin sulfate monoclonal antibody to mediate fluorescence in situ was markedly reduced by absorption with solid-phase chondroitin sulfate proteoglycan that had been chondroitinase ABC-treated, but not by absorption with undigested proteoglycan or with solid-phase heparin. The highly sulfated chondroitin sulfate proteoglycans of rat serosal mast cells are the same type synthesized by the rat mucosal mast cell subclass.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗

PubMed1983

Proteoheparan sulfate from human skin fibroblasts. Evidence for self-interaction via the heparan sulfate side chains.

We have studied the affinity between fibroblast proteoheparan sulfate (medium- and cell surface-derived species) and heparan sulfate-agaroses by affinity chromatography. The evidence for an interaction between the heparan sulfate side chains of the proteoglycans and the immobilized heparan sulfate are as follows: (a) the individual side chains released from the proteoglycan by papain bind to the affinity matrix, (b) the bound proteoglycans are desorbed by a solution of cognate heparan sulfate chains, and (c) the core protein obtained by heparan sulfate-lyase digestion of the proteoglycan does not bind to the affinity matrix. The proteoglycans interact only with one subtype of heparan sulfate. The binding of free heparan sulfate chains to the affinity matrix is completely abolished by heparan sulfate oligosaccharides provided they are composed of both iduronate- and glucuronate-containing disaccharide sequences.

Animals↗

PubMed1981

Self-association of heparan sulfate. Demonstration of binding by affinity chromatography of free chains on heparan sulfate-substituted agarose gels.

We have developed an affinity chromatography procedure which measures binding of heparan sulfate species to agarose gels substituted with different heparan sulfates. Three major subfractions of bovine lung heparan sulfate (HS2, HS3, and HS4) which differ in sulfate content and hexuronate composition have been used. Association-prone variants of these species (HS2-A, HS3-A, and HS4-A) were prepared by gel chromatography. Free heparan sulfate chains were applied to columns of various heparan sulfate-agaroses which were eluted with a linear guanidine gradient and binding was assessed by measuring the hexuronate content of the effluent. Associating heparan sulfate of a particular subfraction was chiefly bound to gels that were substituted with chains of the same kind, i.e. HS2-A to HS2-A-agarose, HS3-A and HS4-A to HS3-A-agarose, and HS4-A to HS4-A-agarose. N-Desulfation and N-acetylation of HS2-A markedly reduced binding to HS2-A-agarose and periodate oxidation of glucuronate in HS3-A completely abolished binding to HS3-A-agarose. Partially oxidized HS2-A was separated into bound and unbound material by affinity chromatography on HS2-A-agarose. Gel chromatography of these fractions indicated that unbound chains were significantly smaller than bound ones. It is concluded that association between heparan sulfate chains may be quite specific and that the strength of binding is dependent on co-operative interactions between a number of contact zones. The latter may correspond to the N-sulfated and iduronate- and glucuronate-containing segments.

Animals↗

PubMed1980

Turbidimetry of inorganic sulfate, ester sulfate, and total sulfur in urine.

We describe simple and precise methods for the determination of inorganic sulfate, ester sulfate, and total sulfur in urine. The methods are based on turbidimetry of sulfate as barium sulfate in the presence of a small amount of preformed barium sulfate and with polyethylene glycol as a stabilizing agent. Inorganic sulfate is directly determined, whereas ester sulfate is measured after removal of inorganic sulfate, followed by acid hydrolysis. Total sulfur is determined after wet oxidation of the sample with nitric acid and perchloric acid in the presence of vanadate as a catalyst. We also report excretion values for healthy persons on a self-selected diet. Men excrete significantly higher amounts of inorganic sulfate and total sulfur than women, but this sex-related difference becomes insignificant if excretion values are expressed relative to creatinine.

Chromatography, Ion Exchange↗

PubMedDate not supplied

Stereoselective sulfation of albuterol in humans. Biosynthesis of the sulfate conjugate by HEP G2 cells.

The objective of this study was to test the utility of the human hepatoma cell line Hep G2 for the biosynthesis of the sulfate conjugate of the beta 2-agonist drug albuterol and to determine the stereo-chemistry of the sulfation reaction. Albuterol was, together with Na(2)35SO4, incubated with Hep G2 cells for 48 hr at 37 degrees C. After precipitation of the inorganic sulfate and protein in the medium, the radiolabeled albuterol sulfate formed was isolated by reversed-phase HPLC. The structure of the sulfate conjugate was determined by liquid secondary ion MS and tandem MS, producing a clear molecular ion and a characteristic fragmentation pattern, respectively. The maximum yield from a 100 mm culture dish was 400 micrograms, sufficient for structure identification as well as for development of stereospecific methodology. Efforts to increase the yields by increasing inorganic sulfate or using dexamethasone as an inducer produced only modest effects. Resolution of the albuterol sulfate enantiomers by HPLC, after chiral derivatization, showed a clear preference for the sulfation of (-)-albuterol. This was also shown in kinetic experiments with the individual enantiomers, using cell homogenates, which gave apparent KM values of 115 microM and 528 microM for (-)- and (+)-albuterol, respectively, with an apparent Vmax value 1.7 times higher for (-)-albuterol. The efficiency of sulfation (Vmax/KM) was thus 7.8-fold higher for the pharmacologically more active (-)-enantiomer. Based on these observations, considerably higher bioavailability of (+)- than of (-)-albuterol may be anticipated after oral or inhaled doses of this drug.(ABSTRACT TRUNCATED AT 250 WORDS)

Albuterol↗

PubMed1998

The role of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease.

Successful treatment of osteoarthritis must effectively control pain, and should slow down or reverse progression of the disease. Biochemical and pharmacological data combined with animal and human studies demonstrate glucosamine sulfate is capable of satisfying these criteria. Glucosamine sulfate's primary biological role in halting or reversing joint degeneration appears to be directly due to its ability to act as an essential substrate for, and to stimulate the biosynthesis of, the glycosaminoglycans and the hyaluronic acid backbone needed for the formation of proteoglycans found in the structural matrix of joints. Chondroitin sulfates, whether they are absorbed intact or broken into their constituent components, similarly provide additional substrates for the formation of a healthy joint matrix. Evidence also supports the oral administration of chondroitin sulfates for joint disease, both as an agent to slowly reduce symptoms and to reduce the need for non-steroidal anti-inflammatory drugs. The combined use of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease has become an extremely popular supplementation protocol in arthritic conditions of the joints. Although glucosamine sulfate and chondroitin sulfates are often administered together, there is no information available to demonstrate the combination produces better results than glucosamine sulfate alone.

Chondroitin Sulfates↗

PubMed2026

Low-pH sulfate reduction in acid mine drainage treatment systems: implications for acidophilic and acid-tolerant sulfate-reducing bacteria - a systematic review.

Acid mine drainage (AMD) is characterized by persistent acidity, high sulfate and dissolved metal concentrations. Sulfate-reducing bacteria (SRB) are attractive candidates for AMD remediation because dissimilatory sulfate reduction generates alkalinity while producing sulfide that can facilitate metal removal through precipitation. Extending these processes to acidic conditions has increased interest in acidophilic and acid-tolerant SRB (aSRB and atSRB), yet evidence from cultivation, molecular surveys and treatment systems has often been interpreted separately. This systematic review synthesized 53 culture-dependent, culture-independent, and treatment system studies from 2014 to 2024 to examine relationships among taxonomic occurrence, physiological capability, demonstrated low-pH sulfate reduction and treatment performance. Phylogenetic analysis showed that low-pH sulfate-reducing phenotypes were distributed across multiple lineages and 16S rRNA relatedness alone did not predict acid tolerance. Desulfosporosinus was the most consistently represented genus across studies, although its recurrence was influenced by cultivation strategies. Sulfate reduction was demonstrated below pH 3, with sustained low-pH activity most strongly supported by controlled reactor studies; approximately pH 4.0-5.5 emerged as a comparatively well-supported range, while activity at lower pH was more dependent on microbial physiology and experimental conditions. Low-pH sulfate reduction also emerged as a community-level process shaped by electron-donor use, metabolite turnover and complementary microbial functions, while treatment performance additionally depended on biomass retention, hydraulic conditions and sulfide management. The reviewed studies support a distinction between taxonomic presence, demonstrated activity and treatment contribution. Future work should prioritize standardized reporting of active sulfate-reduction conditions, stronger taxon-function validation and long-term field testing of low-pH sulfidogenic systems.

Sulfates↗

PubMed1996

Perlecan and basement membrane-chondroitin sulfate proteoglycan (bamacan) are two basement membrane chondroitin/dermatan sulfate proteoglycans in the Engelbreth-Holm-Swarm tumor matrix.

The presence of proteoglycans bearing galactosaminoglycan chains has been reported, but none has been identified previously in the matrix of the Engelbreth-Holm-Swarm tumor, which is a source of several basement membrane components. This tumor matrix contains perlecan, a large, low buoyant density heparan sulfate proteoglycan, widespread in many basement membranes and connective tissues. We now identify two distinct proteoglycan species from this tumor source, which are substituted with galactosaminoglycans and which show basement membrane localization by immunohistochemistry. One species is perlecan but, in addition to being present as a heparan sulfate proteoglycan, it is also present as a hybrid molecule, with dermatan sulfate chains. A minor population of perlecan apparently lacks heparan sulfate chains totally, and some of this is substituted with chondroitin sulfate. The second species is immunologically related to basement membrane-chondroitin sulfate proteoglycan (BM-CSPG) and bears chondroitin sulfate chains. No BM-CSPG was detectable which was substituted with heparan sulfate chains. A combination of immunological and molecular approaches, including cDNA cloning, showed that perlecan and BM-CSPG are distinct in core protein structure. Both are, however, basement membrane components, although there are tissue-specific differences in their distribution.

Animals↗

PubMed1969