Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.6.4 (chondroitinase)
2,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The acidic glycosaminoglycans (AGAG) in normal portions of human gastric tissue were separated by electrophoresis in 3 buffer systems. Paper chromatographic separation of the constitutional disaccharide units by digestion of chondroitin sulfates (CS) with chondroitinase-ABC and chondroitinase-AC was carried out after fractionation of CS by ion-exchange resin column chromatography. Thin-layer chromatography of hexosamines and other biochemical analysis were also performed. The presence of hyaluronic acid in the gastric tissue was substantiated by the enzymatic susceptibility to streptomyces hyaluronidase. The results indicated that human gastric AGAG consisted of, in the order of amount, heparan sulfates, dermatan sulfate, hyaluronic acid, chondroitin-4-sulfate, chondroitin-6-sulfate and presumably oversulfated chondroitin sulfate.
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PMID:A study of acidic glycosaminoglycans in human gastric tissue. 61 34

It was shown that a proteoglycan is synthesised by embryos of a Japanese sea urchin, Hemicentrotus pulcherrimus. This proteoglycan appears as a single peak on sucrose density gradient ultracentrifugation throughout the development. About half of the mucopolysaccharide moiety in this proteoglycan was found to be dermatan sulphate and the rest to be chondroitinase-resistant mucopolysaccharides. Evidence is presented to show that both types of mucopolysaccharide do not exist in a free form but reside as an integral part of the proteoglycan. The linkage between mucopolysaccharide and protein moieties of the proteoglycan appeared not to be an O-glycosidic bond, which is common among other proteoglycans such as proteochondroitin sulphate and proteodermatan sulphate.
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PMID:Appearance of a proteoglycan in developing sea urchin embryos. 66 28

Cytoplasmic granules of basophilic leukocytes stain metachromatically and have been thought to contain sulfated glycosaminoglycans, presumably heparin. To test this hypothesis, we identified the [35S]glycosaminoglycans synthesized by guinea pig blood basophils in culture and in vivo. Basophils isolated from guinea pig blood were cultured for 20 hr in F12 medium--10% guinea pig serum containing sodium [35S]sulfate. Alternatively, basophils were purified from animals receiving repeated i.v. injections of sodium [35S]sulfate. Glycoaminoglycans were isolated from these basophils after pronase digestion and identified by the use of selective glycosaminoglycan-degrading enzymes. Approximately 55% of the [35S]glycosaminoglycans was degraded by chondroitinase AC, indicating the presence of chondroitin sulfate; an additional 30 to 35% could be degraded by chondroitinase ABC, indicating that dermatan sulfate was also present. The 15% glycosaminoglycan remaining after chondroitinase ABC digestion was degraded by purified heparitinase (heparanase), which has no effect on authentic heparin but degrades heparan sulfate. Thus, the glycosaminoglycan content of guinea pig basophils is a mixture of chondroitin sulfate, dermatan sulfate, and smaller amounts of heparan sulfate. No heparin was detected.
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PMID:Sulfated glycosaminoglycans of guinea pig basophilic leukocytes. 68 51

Tetrasaccharides were prepared from chondroitin sulfate by means of a limited degradation with chondroitinase ABC. Tetrasaccharides containing one sulfate per disaccharide unit were isolated and were found to be of three types: a tetrasaccharide with two 6-sulfated disaccharide units, a tetrasaccharide with two 4-sulfated disaccharide units, and a tetrasaccharide with one 4-sulfated disaccharide unit and one 6-sulfated disaccharide unit. Samples of each of these three types of tetrasaccharides were obtained from chick embryo epiphyseal cartilage and from a mixture of bovine tracheal cartilage and shark cartilage. The presence of both a 4-sulfated disaccharide unit and a 6-sulfated disaccharide unit in the same tetrasaccharide molecule indicates the existence of mixed 4 and 6 sulfation on the same chondroitin sulfate chain.
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PMID:Copolymers of chondroitin 4-sulfate and chondroitin 6-sulfate in chick embryo epiphyses and other cartilage. 70 Dec 80

Acidic glycoconjugates (glycosaminoglycans and glycoprotein) were obtained, from myometrium of ovariectomized rabbit under estrogenic condition, by pronase digestion, fractionation with cetylpyridinium chloride and Dowex I column chromatography, in succession. Composition of acidic glycoconjugates was determined enzymatically, employing Streptomyces hyaluronidase, chondroitinase AC II, chondroitinase ABC and crude heparinase. Each glycoconjugate was distributed in 3 approximately 8 fractions obtained by Dowex I column chromatography, indicating its charge and/or molecular heterogeneity. Acidic glycoconjugates consisted of hyaluronic acid (13.4%), chondroitin sulfates A plus C (39.4%), dermatan sulfate (24.6%), heparan sulfate (18.7%) and acidic glycoprotein (most probably sialoglycoprotein) (3.9%). Composition of acidic glycoconjugates in myometrium differed remarkably from that in whole uterus. Myometrium was abundant in chondroitin sulfate isomers (chondroitin sulfates A plus C plus dermatan sulfate), but lacked sulfated glycoprotein. The present results suggested that myometrium and endometrium of uterus may play quite different roles in reproduction.
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PMID:Composition of acidic glycoconjugates (glycosaminoglycans and glycoprotein) in myometrium of rabbit uterus under estrogenic condition. 71 60

Heparin-like glycosaminoglycans (GAG) were isolated from commerical Vessel and their biologic properties studied. Vessel was found to be a mixture of chondroitin sulfates, dermatan sulfate and heparin-like GAG. Chondroitin sulfates and dermatan sulfate in Vessel were hydrolyzed by chondroitinase ABC and the residual Vessel was fractionated on a Dowex-1 Cl- column eluting with a stepwise-increasing concentration of NaCl (1.2--4.0 M). The major fractions eluted at 1.6 M and 1.8 M NaCl were tentatively identified by chemical analysis as heparin-like GAG with somewhat lower sulfate content than standard heparin. Both fractions had lipoprotein lipase-releasing activity and anticoagulant activity similar to heparin, but 1.6 M NaCl fraction had a third of the anticoagulant activity of standard heparin. The 1.8 M NaCl fraction complexed with serum lipoproteins similarly to heparin. In preliminary studies cholesterol-fed rabbits treated with Vessel exhibited somewhat less atherosclerosis than controls.
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PMID:Studies of glycosaminoglycan composition and biologic activity of Vessel, a hypolipidemic agent. 72 39

An 18-year-old boy with oculo-cerebro-renal syndrome excreted a large amount of acid glycosaminoglycans in urine. The identification and characterization of the acid glycosaminoglycans were carried out by the methods of preparative column electrophoresis, ion exchange chromatography, gelfiltration, paper chromatography of the chondroitinase digests and chemical analysis. On admission to hospital, the main components of the urinary acid glycosaminoglycans were undersulfated chondroitin 4-sulfate of large molecular weight and heparan sulfate. Three months after oral administration of the supplement of alkali, the excretion of heparan sulfate and the molecular size of chondroitin 4-sulfate decreased significantly, although the amount of urinary acid glycosaminoglycans remained at a high level (about 25 mg/day). The decrease of heparan sulfate and the shift to a smaller molecule of chondroitin 4-sulfate were coincident with the improvement in clinical and laboratory findings. These results suggest that the abnormal metabolism of acid glycosaminoglycans is a characteristic manifestation in this case and the studies on ground substance metabolism might be an important approach to the pathogenesis of this syndrome.
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PMID:Urinary acid glycosaminoglycans in a patient with oculo-cerebro-renal syndrome. 73 47

Antibodies to collagen in the synovial fluid of RA patients were determined by radioimmuno assay using 14-C-labeled collagen and by passive hemagglutination with collagen coated erythrocytes. The effect of various glycosaminoglycans, possibly present in synovial fluid, on these two assays was investigated. None of the glycosaminoglycan preparations tested significantly changed either antibody titers or the amount of 14-C-radioactivity precipitated in radioimmunoassay. Digestion of the synovial fluid with chondroitinase ABC likewise had no effect on the results. It is therefore concluded that the glycosaminoglycans present in synovial fluid do not interact with native or denatured collagen under the experimental conditions existing in the determination of antibodies to collagen.
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PMID:Effect of glycosaminoglycans on the detection of antibodies to collagen in synovial fluid. 73 53

Monomer proteoglycan was isolated from porcine ovarian follicular fluid by isopycnic CsCl centrifugation in the presence of 4 M guanidine HCl and protease inhibitors. The elution profile of the D1 preparation on Sepharose 2B was similar to that of monomer proteoglycan from bovine nasal cartilage, indicating a similar molecular size. Follicular fluid proteoglycans consist of about 20% protein, 50% dermatan sulfate, and 20% oligosaccharides rich in sialic acid, galactose, mannose, glucosamine, and galactosamine. The amino acid composition of this proteoglycan is significantly different from that of cartilage proteoglycans, with a higher proportion of aspartic acid, threonine, and lysine, and lower amounts of proline and glycine. Alkali-released dermatan sulfate chains are larger on Sepharose 6B (average Mr = 56,000) than chondroitin sulfate chains from cartilage proteoglycans (average Mr = 25,000), and iduronic acid accounts for 9% of total hexuronic acid. Disaccharide units released by chondroitinase ABC consists of 67% 4-sulfated, 22% 6-sulfated, 5% non-sulfated, and 5% disulfated disaccharides. After treatment with 0.05 M NaOH, 1 M NaBH4 at 45 degrees C for 24 h, two major sialic acid-containing oligosaccharides were observed on Sephadex G-25, corresponding to penta- and hexasaccharides. The pentasaccharide contained sialic acid, galactose, glucosamine, and galactosamine in the proportions 1:2:1:1. The galactosamine is O-glycosidically linked to the protein core. This oligosaccharide accounts for approximately 77% of all the sialic acid in the follicular fluid proteoglycans. The hexasaccharide fraction contained sialic acid, galactose, mannose, and glucosamine in the proportions 1:2:1:2. It also contained a small amount of fucose and galactosamine. The linkage of these oligosaccharides to the protein core remains to be determined. The follicular fluid proteoglycans, unlike those from cartilage, do not interact with hyaluronic acid. Digestion with trypsin, chymotrypsin, or plasmin released dermatan sulfate-peptides nearly as small as those released by papain or alkali; in contrast, cartilage proteoglycans were resistant to plasmin and released peptides containing an average of more than four chondroitin sulfate chains after trypsin or chymotrypsin digestion.
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PMID:Isolation and characterization of proteoglycans from porcine ovarian follicular fluid. 76

The chorionic villi of placentas, 10 to 40 weeks of gestation, were examined for A and B blood group antigens with an immunoferritin technique. No specific ferritin attachment was shown on the plasma membrane of the villous trophoblasts. Furthermore, after trophoblast cell-surface mucosubstances (perhaps the barrier of the placental antigenicity, according to some authors) were digested with several enzymes, such as neuraminidase, hyaluronidase, chondroitinase ABC, pepsin, trypsin, and pronase, no ferritin tagging was observed on the plasma membrane of the villous trophoblasts. We have concluded that our failure to detect the A and B blood group antigens was not due to the masking of antigens by mucosubstance coating the trophoblasts, but was due to the intrinsic deficit of those antigens in the plasma membrane of the human trophoblasts.
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PMID:Innumoelectron microscopy of the human chorionic villus in search of blood group A and B antigens. 79 65


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