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PubMed1976

On the structure of heparitin sulfates. Analyses of the products formed from heparitin sulfates by two heparitinases and a heparinase from Flavobacterium heparinum.

The analyses of the products formed from heparitin sulfates by the action of two heparitinases and a heparinase from Flavorbacterium heparinum is reported. Heparitin sulfates A and B are degraded by heparitinase I yielding two disaccharides, one of them composed of N-acetylucosamine and an unsaturated uronic, joined by alpha(1 lead to 4) linkage, and the other, with the same composition but with an O-sulfate at the hexosamine moiety. A third disaccharide is also formed from heparitin sulfate B, by the action of the same enzyme, composed of glucosamine N-sulfate and an unsaturated uronic acid joined probably by alpha(1 lead to 4) linkage. Besides these three disaccharides, heparitin sulfate B yields, by the action of heparitinase I, an oligosaccharide (with an average molecular weight of 6000) which is completely degraded by the heparitinase II yielding a disaccharide composed of glucosamine 2,6-disulfate and unsaturated uronic acid. All the disaccharides are further degraded by alpha-glycuronidase from Flavobacterium heparinum yielding the respective monosaccharides. Based on these and other analyses the possible structures of the heparitin sulfates are proposed.

Acetylglucosamine↗
PubMed1977

Release of O-sulfate groups under mild acid hydrolysis conditions used for estimation of N-sulfate content.

The treatment of chondroitin sulfate isolated from cultured B16 mouse melanoma cells with 0.04 M HCl at 100 degrees C for 90 min released up to 45% of O-sulfate residues as free inorganic sulfate. In addition to the release of inorganic sulfate, extensive degradation of this polysaccharide as well as of cartilage chondroitin sulfate, pig rib cartilage proteoglycan, heparin and hyaluronic acid was also evident under these conditions. The above hydrolysis conditions are used for characterizing 35S-labeled heparan sulfates synthesized by cultured cells and to calculate ratio of N- and O-sulfates in these molecules. Our results suggest that caution is necessary in interpreting the results of mild acid hydrolysis of glycosaminoglycans.

Animals↗
PubMed1979

Absorption, serum levels and urinary excretion of inorganic sulfate after oral administration of sodium sulfate in the conscious rat.

The absorption of inorganic sulfate after ingestion was investigated in rats. After oral administration of Na235SO4, 35S radioactivity was measurable in plasma already after 15 min and its plasma concentration reached a peak after about 1.5--2 h. The 35S-radioactivity excreted in urine during 24 h after ingestion of Na235SO4 together with varying amounts of unlabelled Na2SO4 (0.25--5.0 mmol Na2SO4 per rat) indicated an almost complete absorption of inorganic sulfate from the gastrointestinal tract. Determination of the inorganic sulfate concentration in rat serum 2 h after oral administration of 5.0 mmol Na2SO4 revealed a three-fold increase in serum sulfate concentration. The data suggest a rapid and almost complete absorption of inorganic sulfate after oral administration in the rat. Its importance in relation to the sulfate availability for sulfate conjugation of drugs is discussed.

Administration, Oral↗
PubMed1976

Separation of dermatan sulfate from heparan sulfate in mucopolysaccharidosis urine by chromatography on Sephadex G-75.

Oligosaccharides of testicular hyaluronidase-degraded dermatan sulfate were separated from undegraded dermatan sulfate by chromatography on Sephadex G-75, but not by chromatography on Sephadex G-25. All but the smallest of these oligosaccharides were recovered in excellent yield following dialysis and precipitation with cetyl pyridinium chloride (CPC). G-75 chromatography of dialyzed, concentrated Hunter urine mucopolysaccharides precipitated with CPC resolved most of the large dermatan sulfate into a void volume related peak which was free of heparan sulfate. Decreasing amounts of dermatan sulfate oligosaccharides were eluted with sephadex-retarded polysaccharides, including small amounts which appeared with otherwise pure heparan sulfate.

Child↗
PubMed1977

Structural characteristics of heparan sulfates with varying sulfate contents.

Structural properties of heparan sulfate preparations from hog mucosa and beef lung sources were obtained by application of Smith degradation and nitrous acid reactions. Products formed by these reactions indicated that most of the iduronic acid present in these mucopolysaccharides is ester sulfated, whereas N-sulfated glucosamine residues are ester sulfated much less frequently. Repeating units with sulfated iduronic acid found to occur almost entirely in single sequences. Futhermore, the iduronic acid moieties may be bound to either N-acetylated or N-sulfated glucosamine units, with these occuring at either end of the uronic acid unit.

Animals↗
PubMed1975

The distribution of sulfated uronic acid and hexosamine residues in heparin and heparan sulfate.

Heparins from various sources and heparan sulfate from umbilical cords have been subjected to Smith-degradation and reaction with nitrites. These procedures were effective for providing data relating to the distribution of sulfated iduronic acid residues in the molecule. Results indicated that heparins may have, as a prominent structural feature of the molecule, non-sulfated uronic acid distributed in single sequences, much as had been shown previously for N-acetylglucosamine residues. Sulfated uronic acid, however, may occur in multiple sequences of up to 5 or 6 residues. Heparan sulfate was found to have a major proportion of its ester sulfate on iduronic acid rather than hexosamine units, thereby having sections similar to those in heparins, though in considerably lower proportion.

Amino Acids↗
PubMed1979

The occurrence of uridine diphosphate N-acetylgalactosamine 6-sulfate in quail egg white and characteristic distribution of sulfated sugar nucleotides in different avian eggs.

A sulfated sugar nucleotide has been isolated from quail egg white, and accounts for nearly 80% of the total sugar nucleotides found in the egg white. Evidence is presented that this nucleotide is uridine diphosphate N-acetylgalactosamine 6-sulfate, an isomer of the 4-sulfated derivative of uridine diphosphate N-acetylgalactosamine previously found in chicken egg white. Further studies on the distribution of sulfated sugar nucleotides in egg white of various birds (chicken, quail, pheasant, peafowl, turkey, goose, and duck) demonstrate that each species has a characteristic composition, differing from one another regarding the relative amounts of 4-sulfated, 6-sulfated, and 4,6-bissulfated derivatives of uridine diphosphate N-acetylgalactosamine.

Animals↗
PubMed1975

Biochemical studies on sulfate-reducing bacteria. XIV. Enzyme levels of adenylylsulfate reductase, inorganic pyrophosphatase, sulfite reductase, hydrogenase, and adenosine triphosphatase in cells grown on sulfate, sulfite, and thiosulfate.

Sulfate-reducing bacteria, Desulfovibrio vulgaris, strain Miyazaki, were grown on either sulfate, sulfite, or thiosulfate as the terminal electron acceptor. Better growth was observed on sulfite and less growth on thiosulfate than on sulfate. Enzyme levels of adenylylsulfate (APS) reductase [EC 1.8.99.2], reductant-activated inorganic pyrophosphatase [EC 3.6.1.1], sulfite reductase [EC 1.8.99.1] (desulfoviridin), hydrogenase [EC 1.12.2.1], and Mg2+-activated ATPase [EC 3.6.1.3] were compared in crude extracts of these cells at various stages of growth. 1) The specific activity of APS reductase in sulfite-grown cells was only one-fourth that in sulfate-grown cells throughout growth. Thiosulfate-grown cells had an activity intermediate between those of sulfate- and sulfite-grown cells. 2) Cells grown on sulfite had lower specific activity of reductant-activated inorganic pyrophosphatase than cells grown on sulfate or thiosulfate. 3) The specific activity of sulfite reductase (desulfoviridin) was highest in sulfite-grown cells. The sulfite medium gave the enzyme in high yield as well as with high specific activity. 4) The specific activities of hydrogenase and Mg2+-ATPase were not significantly altered by electron acceptors in the growth medium.

Adenosine Monophosphate↗
PubMed1976

Effect of cholesterol sulfate and sodium dodecyl sulfate on lecithin-cholesterol acyltransferase in human plasma.

The effects of cholesterol sulfate and sodium dodecyl sulfate (SDS) on the esterification of cholesterol in sonicated dispersions of lecithin-cholesterol mixtures by lecithin-cholesterol acyltransferase [EC 2.3.1.43] (LCAT) in human plasma were studied in vitro. The acyltransferase activity was inhibited at concentrations of cholesterol sulfate higher than 1 X 10(-4) M. This inhibition was not eliminated by the addition of bovine serum albumin or CaC12. On the contrary, the acyltransferase activity was stimulated at concentrations of SDS ranging from 1 X 10(-5) M to 1 X 10(-3) M, and maximum stimulation was obtained at 5 X 10(-4) M. The maximum stimulation disappeared on the addition of bovine serum albumin (30 mg per ml of incubation medium), 1 X 10(-3) M CaC12 or 1 X 10(-4) M cholesterol sulfate. On the other hand, the extent of inhibition of the acyltransferase by cholesterol sulfate was not affected by the amount of lecithin in the dispersion added as a substrate, but the maximum stimulation (5 X 10(-4) M SDS) of the acyltransferase was interfered with when a large amount of lecithin was present in the dispersion. In addition, the amount of SDS required for maximum cholesterol esterification was not affected by the amount of lecithin present in the dispersion. These results suggest that the action of cholesterol sulfate on the acyltransferase is different from that of SDS.

Acyltransferases↗
PubMed1975

Purification of Keratan Sulfate-endogalactosidase and its action on keratan sulfates of different origin.

A glycosidase which attacks corneal keratan sulfate was purified from extracts of Pseudomonas sp. IFO-13309. When corneal keratan sulfate was degraded by the purified enzyme, Sephadex G-50 chromatography indicated the presence of a number of oligosaccharides differing in size and sulfate content. The characterization of two major fractions of the oligosaccharides indicated that the point of enzyme attack is limited to the endo-beta-D-galactoside bonds in which nonsulfated D-galactose residues participate. The enzyme, unlike ordinary exo-beta-D-galactosidases, did not catalyze the hydrolysis of phenyl beta-D-galactoside. Moreover, beta-D-galactosyl-(1 leads to 3)-2-acetamido-2-deoxy-beta-D-glucosyl-(1 leads to 3)-beta-D-galactosyl-(1 leads to 4)-D-glucose ("lacto-N-tetraose") was completely refractory to the action of this enzyme, suggesting that a structure of the type, X-(1 leads to 3)-beta-D-galactosyl-(1 leads to 4)-Y, is not the only specificity-determining factor, i.e. neighboring sugars, X and Y, or even larger portions of substrate molecule must have an important effect. Compared with corneal keratan sulfate, keratan sulfates from human nucleus pulposus and shark cartilage were attacked at lower rates with a resultant production of oligosaccharides of relatively large size. The result is in agreement with the view that considerable variations exist in the structure of keratan sulfates of different origin, and further suggests that the enzyme may serve as a useful reagent in studying these variations.

Aged↗
PubMed1976

Degree of sulfation in mucopolysaccharide sulfates in normal and stone-forming urines.

Mucopolysaccharides were extracted from both normal and stone-forming urines, and those from the stone-forming samples showed a higher degree of sulfation than those from normal urines, as determined by sulfate analysis and electrophoretic measurement. The sulfated mucopolysaccharides from stone-forming urines formed insoluble calcium salts, whereas those from normal urines generally remained soluble in the presence of calcium ion. Rachitic rat cartilage was found to have more highly sulfated mucopolysaccharides than normal rat cartilage. Highly sulfated mucopolysaccharides appear to be a significant factor in calcium stone formations.

Animals↗
PubMed1978

A low-sulfated chondroitin sulfate in rat blood: an acidic glycosaminoglycan with a high metabolic rate.

The rate of metabolism of low-sulfated chondroitin 4-sulfate, a predominant glycosaminoglycan in blood, has been studied by administering intraperitoneally radioactive hexosamine and/or sulfate to rats. The biological half-life of the material was estimated to be 10--12 h, suggesting that the metabolic process of blood low-sulfated chondroitin sulfate is different from that of glycosaminoglycans in the tissue.

Animals↗
PubMed1978

Comparison of in vivo and in vitro responses to sulfated and non-sulfated ceruletide.

Responses of, guinea pig gall bladder to sulfated and non-sulfated ceruletide were compared in vitro and in vivo. Tested in vivo, sulfated ceruletide was 75 times more potent than non-sulfated. In vitro, sulfated was 150 times more potent. Thus, differences in potency are substantially less when tested in vivo, and reported differences in relative potency reflect not only chemical structure but also the method used for testing.

Animals↗
PubMed1978

Cholecystokinin (pancreozymin). 4. Synthesis and properties of a biologically active analogue of the C-terminal heptapeptide with epsilon-hydroxynorleucine sulfate replacing tyrosine sulfate.

The influence of tyrosine O-sulfate, the 27th residue in the sequence of cholecystokinin (pancreozymin) (CCK-PZ), on the contraction of gall bladder of guinea pigs and on the release of amylase in isolated pancreatic cells of the same animal was studied with an analogue of the biologically active C-terminal heptapeptide, CCK-PZ-(27--33). In the new analogue, tyrosine O-sulfate was replaced by epsilon-hydroxynorleucine O-sulfate. The synthetic peptide was found a full agonist in these tests, not quite as potent as the unaltered heptapeptide, but much more active than the previously prepared and studied serine O-sulfate containing analogue. Thus, the distance of the sulfate ester group from the peptide backbone has a major influence on the biological activity of CCK-PZ.

Amino Acid Sequence↗
PubMed1979

Isolation and partial characterization of low sulfated chondroitin 4-sulfate-proteoglycan in bovine blood.

Bovine plasma low sulfated chondroitin sulfate-proteoglycan (34 microgram/ml plasma), accounting for the main component of acidic glycosaminoglycans in blood, has been purified by isoelectric precipitation, dissociation with 4 M guanidine chloride followed by DEAE-chromatography, Sephadex G-200 chromatography and by preparative polyacrylamide gel electrophoresis. The proteoglycan, having a molecular weight of approx. 44,000, is composed of about 77% protein and 23% glycosaminoglycan at a molar ratio of 1 : 1 which could be cleaved by alkaline treatment into each component. Amino acid analysis of the proteoglycan and its glycosylpeptide has shown that the material is derived from a different origin from other tissue proteoglycans, though the amino acid residues surrounding O-glycosidic linkage to serine residue are quite similar to that of cartilage proteoglycan. Characteristic features of plasma low sulfate chondroitin sulfate-proteoglycan are discussed, compared with tissue materials.

Amino Acids↗
PubMed1975

Kinetics of sulfate transport by Penicillium notatum. Interactions of sulfate, protons, and calcium.

The active transport of inorganic sulfate by an ATP sulfurylase-negative strain of Penicillium notatum is promoted by H+ ions and metal ions (divalent metal ions being more effective than monovalent metal ions). Initial velocity studies suggest that H+ and SO4(2-) add to the carrier in an ordered sequence (H+ before SO4(2-)), with H+ at equilibrium with free carrier and carrier-H+ complex. The linear reciprocal plots and replots suggest a 1:1 stoichiometry between H+ and SO4(2-). Ca2+ and other divalent metal ions stimulate sulfate transport markedly in buffered suspensions of low ionic strength. The kinetics of the Ca2+/SO4(2-) interaction suggest that Ca2+ (like H+) adds to the carrier before SO4(2-) and is at equilibrium with free carrier and carrier-Ca2+ complex. The linear reciprocal plots and replots indicate a 1:1 stoichiometry between Ca2+ and SO4(2-). Thus the fully loaded carrier-SO4(2-) -Ca2+ -H+ complex has a net positive charge relative to that of the free carrier, a fact consistent with the chemiosmotic hypothesis of membrane transport. The kinetics of the H+/Ca2+ interaction point to a random A-B (rapid equilibrium), ordered C sequence with A = H+, B = Ca2+, and C = SO4(2-). Selenate (an alternate substrate competitive with sulfate) is an uncompetitive inhibitor with respect to Ca2+, in agreement with the suggested mechanism. Internal charge balance is not accomplished by a stoichiometric coaccumulation of Ca2+ and SO4(2-). Sulfate transport does, however, promote 45Ca2+ uptake. A significant fraction of the added Ca2+ is bound by the mycelial surface. Binding is extremely rapid, but reversible.

Binding, Competitive↗
PubMed1977

Chemistry of the sulfate groups in a sulfated glycoprotein from rabbit submandibular gland.

A 35S-labeled sulfated glycoprotein was isolated from rabbit submandibular glands. Acid stability studies on the 35sulfate groupings present in the intact glycoprotein gave a half-life of 45 min. Partial acid hydrolysis of the 35S-labeled glycoprotein in 0.1 M HC1 for 90 min at 100 degrees C liberated a radioactive fraction which was free from peptide and fractionated in the monosaccharide range of a Sephadex G-15 column. Examination of this fraction by paper chromatography revealed the presence of a major component having the characteristics of N-acetylglucosamine 6-0-sulfate and a minor component having the properties of N-acetylgalactosamine 6-0-sulfate. The presence of ester sulfate groups in the intact glycoprotein was confirmed by infrared spectroscopy.

Animals↗
PubMed1978

Site of emetic action of oral copper sulfate in dogs. (I) Thresholds of various portions of gastrointestinal tract to locally applied copper sulfate.

Emetic thresholds to copper sulfate administered into the Pavlov pouch, Forrest pouch, Thiry fistulas of the jejunum and ileum, and duodenal, jejunal and ileal catheters were measured in dogs to conjecture the site of emetic action of copper sulfate. The oral emetic threshold had been measured preoperatively. In the stomach, the pyloric antrum had a high sensitivity, while the corpus had a low sensitivity to the topically applied copper sulfate. In the intestine, the sensitivity was high in the duodenum, whereas a low sensitivity was noted in the jejunum. Almost no sensitivity was observed in the ileum. Thus it would appear that the site of the emetic action of copper sulfate was the pyloric antrum and/or duodenum.

Administration, Oral↗