Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.36 (hyaluronidase)
4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Urea treatment of a temperate bacteriophage from a type 49 strain of group A streptococcus (Streptococcus pyogenes) followed by ammonium sulfate fractionation, ion exchange, and affinity chromatography of solubilized proteins provided for the recovery (12%) and purification (44-fold) of the phage-associated hyaluronidase. The molecular weight of the homogeneous, purified enzyme was estimated to be 71,000 by polyacrylamide gel electrophoresis (in the presence of sodium dodecyl sulfate) and 75,000 by gel filtration with Sephacryl S-200. The enzyme has a pH optimum of 5.5, a Vmax of 0.1 absorbance unit/min per microgram of protein, and a Km of 4.8 X 10(-2) mg/ml with umbilical cord hyaluronic acid as substrate. Of the cations tested, calcium and magnesium were the only effectors of the enzyme. The enzyme is a glycoprotein (7.25% carbohydrate) containing glucose, galactose, and glucosamine. Analysis of the amino acid composition revealed a predominance of acidic amino acids and a relatively high content of cysteine. The partial specific volume, estimated from the amino acid and sugar analyses, was 0.725 cm3/g.
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PMID:Purification and characterization of a hyaluronidase associated with a temperate bacteriophage of group A, type 49 streptococci. 2 84

By light microscopy the subdermal nodule of a patient with fibrodysplasia ossificans progressiva (FOP) had a fibromatoid histologic appearance. The cytoplasm of the cells stained strongly for mannose-rich glycoprotein with the concanavalin A-horseradish peroxidase (con A-HRP) method. The tumors also exhibited abundant hyaluronidase-digestible mucopolysaccharide in the interstitium with various basic staining reagents. This material appeared to consist principally of hyaluronic acid or chondroitin sulfate with few or mainly masked sulfate esters. At the ultrastructural level, cells interpreted as the tumor cells in the subdermal nodule from the patient displayed extremely hyperplastic granular reticulum and well-developed Golgi elements and appeared very active in synthesis and secretion of protein. The material in the dilated cisternae of the granular reticulum stained for glycoprotein with the con-A-HRP method. Macrophages which comprised the other main cell type in the nodules commonly contacted the tumor cells and occasionally evidenced engulfment of these cells. The intercellular matrix of the nonossified subdermal nodule exhibited greatly increased mucosubstance and, by electron microscopy, showed an unusual network of dialyzed iron-reactive acid muco-substance in the interstitium.
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PMID:Histochemical and ultrastructural studies in fibrodysplasia ossificans progressiva (myositis ossificans progressiva). 14 Dec 14

Rat liver cells grown in primary cultures in the presence of [(35)S]sulphate synthesize a labelled heparan sulphate-like glycosaminoglycan. The characterization of the polysaccharide as heparan sulphate is based on its resistance to digestion with chondroitinase ABC or hyaluronidase and its susceptibility to HNO(2) treatment. The sulphate groups (including sulphamino and ester sulphate groups) are distributed along the polymer in the characteristic block fashion. In (3)H-labelled heparan sulphate, isolated after incubation of the cells with [(3)H]galactose, 40% of the radioactive uronic acid units are l-iduronic acid, the remainder being d-glucuronic acid. The location of heparan sulphate at the rat liver cell surface is demonstrated; part of the labelled polysaccharide can be removed from the cells by mild treatment with trypsin or heparitinase. Further, a purified plasma-membrane fraction isolated from rats previously injected with [(35)S]sulphate contains radioactively labelled heparan sulphate. A proteoglycan macromolecule composed of heparan sulphate chains attached to a protein core can be solubilized from the membrane fraction by extraction with 6m-guanidinium chloride. The proteoglycan structure is degraded by treatment with papain, Pronase or alkali. The production of heparan [(35)S]sulphate by rat liver cells incubated in the presence of [(35)S]sulphate was followed. Initially the amount of labelled polysaccharide increased with increasing incubation time. However, after 10h of incubation a steady state was reached where biosynthetic and degradative processes were in balance.
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PMID:Structure and metabolism of rat liver heparan sulphate. 14 28

Lectins (phytohaemagglutinin) are known to have the unique property of binding with certain specific sugars, polysaccharides and glycoproteins. Although the kinetics of interaction between lectins and sugar have been extensively studied, the binding characteristics of the lectins with various glycoproteins are not well understood. In this laboratory a systematic study has been initiated in relation to the interaction of lectins with glycoproteins. Concanavalin A is known to bind alpha-glucosides, mannosides and biopolymers having these sugar configurations. A galactose binding protein from caster bean has been purified to homogeneity and was found to contain mannose. This lectin was used as the source of glycoprotein for studying its interaction with concanavalin A. This study showed that the interaction is temperature dependent and the dissociation is time and alpha-methyl glucoside concentration dependent. This has led to speculate a model for cell-lectin interaction. Using concanavalin A it has been shown that all the lysosomal enzymes from brain studied were glycoprotein in nature. Moreover, using Sepharose-bound concanavalin A it has been possible to devise a method by which these lysosomal enzymes could be purified considerably. With the knowledge that the interaction between lectin and glycoprotein is not only dependent on the specific sugar present in the glycoprotein, but also on the nature of the glycoprotein it was possible to develop a novel method for immobilizing various glycoprotein enzymes, such as arylsulphatase A, hyaluronidase and glucose oxidase.
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PMID:Studies on the interaction of concanavalin A with glycoproteins. 23 36

1. The total content of neutral sugars in skin of the weanling albino rats kept on the protein-deficient diet was increased by about 40%; this was mainly due to the increased concentration of galactose. The content of sialic acid was increased by about 20%. The collagen nitrogen was decreased significantly, with a concomitant increase of non-collagen nitrogen. At the same time, the content of sulphated glycosaminoglycans in skin was significantly decreased and that of non-sulphated glycosaminoglycans was increased. 2. Protein-deficient diet enhanced the activities of the protein-bound carbohydrate-degrading lysosomal hydrolases, viz. cathepsin D (EC 3.4.4.23), N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30) and beta-D-glucuronidase (EC 3.2.1.31) both in liver and skin. The activity of liver hyaluronidase (EC 3.2.1.35) was also increased upon limitation of protein supply. 3. The changes observed in skin were accompanied by increased concentration of the protein-bound hexoses, hexosamines and sialic acids in serum, and of hexosamine and uronic acid in urine. The serum fucose remained unchanged.
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PMID:Effect of protein deficiency on the metabolism of glycoproteins and glycosaminoglycans in albino rat skin. 54 53

A new method for obtaining highly purified hyaluronidase (hyaluronate glycanohydrolase EC 3.2.1.25) in high yield is described. Bull seminal plasma was fractionated with (NH4)2 SO4 and the 30 to 65% saturation fractions were applied to a DEAE-cellulose column. The first protein peak contained hyaluronidase, beta-N-acetylglucosaminidase and beta-glucuronidase. The latter two enzymes were separated by gel filtration on Sephadex G-200. The hyaluronidase was further purified by a Concanavalin-A Sepharose 4B affinity column. By gradient elution with alpha-methyl-D-glucoside a fraction which had a specific activity of 1998 units/mg protein (57 942 National Formulary Standard units/mg protein) was obtained. The highly purified enzyme showed one major protein band on acrylamide gel electrophoresis at pH 4.3. The purified hyaluronidase did not show any beta-glucuronidase or beta-N-acetylglucosaminidase activities. The percent yield of purified hyaluronidase calculated on the basis of total activity was ten times higher than by any pervious method [Yang, C.H. and Srivastava, P.N. (1975) J. Biol. Chem. 250, 79-83].
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PMID:Purification of bull sperm hyaluronidase by concanavalin-A affinity chromatography. 114 14

Effect of various sugars related to cell membrane on the aggregation of HeLa-S3 cells was examined in a rotation culture by adding each sugar to the culture medium. Some specific sugars among those tested induced (1) greater size of aggregates and (2) higher synthesis of hyaluronic acid than that of the control. Since the addition of hyaluronidase inhibited the aggregate formation, both in the test and control cultures, with HeLa-S3 cells of both groups forming only small aggregates, it was presumed that the hyaluronic acid synthesized might be of cardinal importance for the formation of aggregates. The specific sugars producing the effect mentioned above were N-acetyl-D-glucosamine, bis(N-acetyl)chitobiose, N-acetyl-D-galactosamine, alpha-methyl-D-glucopyranoside, and N-acetyl-D-mannosamine, while D-glucosamine, beta-methyl-D-glucopyranoside, L-fucose, D-glucose, and a commercially available hyaluronic acid were ineffective. The findings obtained in the present study interestingly ran parallel with the results of previously reported study on the induction of specific biological phenomena by the cell membrane-related sugars.
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PMID:Stimulation of HeLa-S3 cell aggregation by sugars related to cell membrane in rotation culture. 118 Dec 27

To generate xyloside-primed dermatan sulfate suitable for sequence analysis, skin fibroblasts were incubated with p-hydroxyphenyl-beta-D-xylopyranoside and [3H]galactose, and free [3H]glycosaminoglycan chains were isolated from the culture medium by ion exchange and gel chromatography. After 125I labelling of their reducing-terminal hydroxyphenyl groups, chains were subjected to various chemical and enzymatic degradations, both partial and complete, followed by gradient polyacrylamide gel electrophoresis and autoradiographic identification of fragments extending from the labelled reducing-end to the point of cleavage. Results of periodate oxidation-alkaline scission indicated that the xylose moiety remained unsubstituted at C-2/C-3; exhaustive treatment with chondroitin AC-I lyase afforded the fragment delta HexA-Gal-Gal-Xyl-R (R = radio-iodinated hydroxyphenyl group), and complete degradations with chondroitin ABC lyase as well as testicular hyaluronidase yielded the fragments delta HexA/HexA-GalNAc-GlcA-Gal-Gal-Xyl-R with or without sulfate on the N-acetylgalactosamine. Partial digestions with testicular hyaluronidase or chondroitin B lyase indicated that glucuronic acid was common in the first three repeats after the linkage region and that iduronic acid could occupy any position thereafter. Hence, there were no indications of a repeated, periodic appearance of the clustered GlcA-GalNAc repeats which was previously observed in proteoglycan derived dermatan sulfate [Fransson L-A, Havsmark B, Silverberg I (1990) Biochem J 269:381-8], suggesting a role for the protein part in controlling the formation of particular copolymeric features during glycosaminoglycan assembly.
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PMID:Sequence analysis of p-hydroxyphenyl-O-beta-D-xyloside initiated and radio-iodinated dermatan sulfate from skin fibroblasts. 139 65

We isolated mucin-like glycoproteins from the conditioned medium of primary hamster tracheal epithelial (HTE) cell culture and characterized them biochemically and immunologically. These glycoproteins were purified on Sepharose CL-4B after Streptomyces hyaluronidase treatment and then by CsCl-density-gradient centrifugation in the presence of 4 M-guanidinium chloride. The purified glycoproteins were resistant to digestion by chondroitin AC lyase, heparinase, heparitinase and endo-N-acetylglucosaminidases A, D and H, but susceptible to endo-beta-galactosidase and keratanase. SDS/PAGE demonstrated no contamination by low-molecular-mass proteins. The purified glycoproteins showed a peak buoyant density of 1.56 g/ml in CsCl-density-gradient centrifugation, and contained 10% peptide and 90% carbohydrate by weight. Carbohydrates in these glycoproteins contained N-acetylglucosamine, N-acetylgalactosamine, galactose, fucose, sialic acid and a trace amount of mannose, but no uronic acid. Serine and threonine together accounted for 27% of the total amino acid residues. In addition, the mucin-like glycoproteins exhibited blood-group A and B activities, and very strong inhibitory activity for influenza A virus haemagglutination. With the use of the purified glycoprotein as an antigen, six monoclonal antibodies that stained mucus granules in hamster tracheal epithelium were obtained. We characterized the antibody produced by one of the clones, HM D46. We conclude that HTE cells cultured in the serum-free medium secrete a glycoprotein with physicochemical properties similar to those known in various airways mucins.
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PMID:Mucin-like glycoprotein secreted by cultured hamster tracheal epithelial cells. Biochemical and immunological characterization. 165

Cultures of normal human tracheal gland epithelial cells that exhibit functional differentiation have been propagated in serum-free medium supplemented with insulin (5 micrograms/ml), epidermal growth factor (10 ng/ml), hydrocortisone (0.5 micrograms/ml), and bovine pituitary extract (25 micrograms/ml). The cells retain many characteristics of epithelial cells including microvilli on cell surfaces, desmosomes between cells, and tonofilaments in the cytoplasm. In addition, they exhibit keratin-positive titers and react positively with Peanut agglutinin, which is specific for the disaccharide beta-D-galactose-(1----3)N-acetyl D-galactosamine, a major component of mucin glycoprotein. The cells also exhibit normal Cl- channel activity which was enhanced by the cAMP agonist Forskolin. The major component of the cellular secretion was hyaluronic acid; approximately 10% of the void volume material was resistant to hyaluronidase and may contain material similar to mucin glycoprotein. Some of the cell cultures have been maintained in serum-free conditions for 6 to 7 passages. This model will be important to study regulation of ion-channel activities and mucous glycoprotein secretion and to compare such regulations with the tracheal mucosal epithelial cells already established.
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PMID:Characterization of epithelial cell cultures derived from human tracheal glands. 170 7


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