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:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antiserum to the inhibitor of beta=glucuronidase isolated from porcine sublingual gland was prepared in rabbits. Double immunodiffusion with the inhibitor produced a single precipitin line. However, neutralization of the inhibitor was produced by the antiserum and also by normal serum. Anti-beta-glucuronidase inhibitor isolated from human serum, by fractionation with (NH4)2 SO4 followed by DEAE-cellulose, Sephadex G-200 and Sepharose 4B chromatography, was identified as alpha2-macroglobulin by using ultracentrifuge analysis and immunoelectrophoresis. The mechanism of interaction of beta-glucuronidase inhibitor with alpha2-macroglobulin was also studied.
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PMID:Immunochemical study of beta-glucuronidase inhibitor from porcine sublingual gland. Interaction of beta-glucuronidase inhibitor with alpha2-macroglobulin. 5 72

Following removal of sialic acid by neuraminidase treatment the activity of the beta-glucuronidase inhibitor was remarkably decreased, but the antigenic determinant was not affected. A partial common antigen to the inhibitor was isolated from porcine small intestine, by successive fractionation of trypsin extraction of the latter on Sephadex G-150, DEAE-cellulose and Sepharose 4B column chromatography. The immunologic and characteristic properties of the common antigen were compared with those of the beta-glucuronidase inhibitor is not identical with its antigenic determinant.
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PMID:Immunochemical study of beta-glucuronidase inhibitor from porcine sublingual gland. Relationship between the antigenic determinant and the active site of the inhibitor. 6 58

1. The elution profiles of eleven acid hydrolases from human liver and plasma were directly compared using a system whereby a single salt gradient was simultaneously applied to two DEAE-cellulose chromatographic columns. 2. Plasma alpha-L-fucosidase, alpha-mannosidase, alpha-galactosidase and alpha-glucosidase isoenzymes were eluted at higher salt concentrations than the corresponding liver isoenzymes whereasbeta-N-acetylglucosaminidase, beta-galactosidase, beta-glucosidase, exo-1,4-beta-xylosidase and alpha-L-arabinofuranosidase isoenzymes were eluted at lower salt concentrations. The elution profiles of beta-glucuronidase and acid phosphatase weremore complex. 3. After incubation with neuraminidase most plasma hydrolases were eluted at lower salt concentrations, however the elution patterns of beta-glucosidase, beta-xylosidase and acid phosphatase were not altered. 4. Preincubation with neuraminidase had no effect on the elution profiles of six liver hydrolases whereas the major isoenzymes of alpha-mannosidase, beta-galactosidase and alpha-L-arabinofuranosidase were eluted at markedly lower salt concentrations. Liver alpha-fucosidase and alpha-galactosidase were eluted at slightly lower salt concentrations afterincubation with neuraminidase. 5. The results are discussed in relation to thepathogenesis of Mucolipidosis II (I-cell disease), and the synthesis and packaging of lysosomal enzymes.
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PMID:Effect of neuraminidase on the chromatographic behaviour of eleven acid hydrolases from human liver and plasma. 19 Dec 58

Beta-Glucuronidase has been purified from mouse kidneys previously induced by gonadotrophin to a specific enzyme activity 15 times higher than the non-induced kidney. The purification procedure includes ultrasonication to solubilize the enzyme, acid and ammonium sulfate precipitations, gel filtration in Sephadex G-200, DEAE-ion exchange chromatography, and isoelectric focusing. The resulting product has a specific activity of 284,000 Fishman units/mg of protein, representing a 1,090-fold purification and is 17,000-fold higher than the level in the non-induced kidney. The purified beta-glucuronidase is apparently homogeneous by criteria of gel filtration, sodium dodecyl sulfate gel electrophoresis, and immunodiffusion. Characterization of the purified enzyme showed that it is identical with the lysosomal isoenzymic from electrophoretically, has subunit molecular weight of 74,000 (estimated by sodium dodecyl sulfate gel electrophoresis) and oligomer molecular weight of 300,000. The purified enzyme is stable at high temperature (up to 55 degrees) and at wide range of pH (from 4 to 11). It has a pH optimum for its activity at 4.7 and a Km of 1.18 times 10- minus 4 M. The purification and characterization of this enzyme from mouse kidney will have significance in the understanding of the molecular nature of the isoenzymes of beta-glucuronidase and will be useful in future studies on the mechanism of intracellular transport and distribution of this hydrolase.
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PMID:Purification and characterization of mouse kidney beta-glucuronidase. 23 11

1. Hemolymph from the giant African snail Archachatina marginata has been analyzed for its content of certain lysosomal hydrolases and shown to contain substantial quantities of acid phosphatase (285 units/ml) hexosaminidase (512 units per ml) and beta-glucuronidase (28 units/ml). 2. Hemolymph acid phosphatase can be fractionated into 6 active components by DEAE-Sephadex chromatography. 3. Some of the acid phosphatase species can be distinguished on the basis of heat stability, pH dependency and sensitivity to inhibitors including phosphate, L(+) tartrate, fluoride, formaldehyde and 1.10 phenanthroline.
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PMID:Demonstration of multiple forms of acid phosphatase in hemolymph of the African snail, Archachatina marginata. 31 14

The occurrence of the two molecular forms, I and II, in the beta-glucuronidase of the liver (hepatopancreas) from the marine mollusc Littorina littorea L. has been demonstrated for the first time. The two forms have been purified 355-fold and 1262-fold, respectively. Form I and II of beta-glucuronidase behave differently on DEAE-cellulose chromatography, polyacrylamide gel disc electrophoresis, isoelectric focusing (pH 5.5 and 4.2, respectively), optimum pH (4.4 and 3.4--4.1, respectively), thermal stability, Km (1.2 mM and 0.5 mM with p-nitrophenyl beta-D-glucuronide, 0.3 mM and 0.15 mM with phenolphthalein beta-D-glucuronide as substrates for form I and II, respectively) and V. Their molecular weight, estimated by gel filtration through Sephadex G-200, was about 250000 for both forms. Several subunits were separated by polyacrylamide gel electrophoresis in presence of sodium dodecyl sulphate. This beta-glucuronidase is a glycoprotein, but sialic acid(s) were not detected. The enzyme was very active on synthetic substrates and also on hexasaccharides and tetrasaccharides containing glucuronic acid residues with beta 1 leads to 3 linkages; it had practially no activity on certain glycosaminoglycans. Hg2+ and glucaro-1,4-lactone were very effective inhibitors of this enzyme; the latter by a competitive mechanism.
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PMID:Properties of two molecular forms of beta-glucuronidase from the mollusc Littorina littorea L. 42 83

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

We intend to purify beta-glucuronidase from human liver in a large quantity in order to facilitate the study of its biochemical structure and pathophysiologic roles in cholelithiasis and carcinogenesis. The initial purification procedure involved: (1) liver homogenization, (2) 25-45% saturated ammonium sulfate fractionation, (3) heat denaturation of protein at 56 degrees C, (4) gel filtration with Bio-Gel P-300 gel, (5) anion exchange chromatography with DEAE agarose, (6) cation exchange chromatography with CM agarose, and (7) hydroxyapatite chromatography (overall yield, 1%; overall purification, 169X). The final product was used to immunize rabbits and BALB/c mice for production of polyclonal and monoclonal antibodies, respectively. The antibodies, mainly IgG, were purified by using gamma-Protein A agarose column chromatography. The purified IgG, after periodate oxidation, was coupled to hydrazide gel by formation of a stable covalent hydrazone bond linkage. The new purification procedure involved the initial first three steps, followed by (4) polyclonal IgG immunoaffinity chromatography and (5) monoclonal IgG immunoaffinity chromatography (overall yield, 6.1%; overall purification, 3720X). Polyacrylamide gel electrophoresis indicated minor contaminants in the final product which could be further purified by electroelution. It is concluded that beta-glucuronidase constitutes 0.016 mg per gram of wet liver tissue and can be obtained on a large scale in a highly purified form within a 2-day cycle.
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PMID:A large-scale purification of beta-glucuronidase from human liver by immunoaffinity chromatography. 177 14

Using chondroitin as a substrate, a new type of exo-beta-glucuronidase (EC 3.2.1.31) from rabbit liver was purified using a combination of ammonium sulfate fractionation, DEAE-cellulose chromatography, gel filtration on Sephracryl S-300, affinity chromatography through heparin-Sepharose CL-6B, and preparative polyacrylamide gel electrophoresis. This enzyme acts only on non-sulfated glycosaminoglycans and their oligosaccharides and was shown to be quite different from exo-beta-glucuronidase, which does act on p-nitro-phenyl-beta-D-glucuronide with regard to the following properties. 1) Neither sulfated glycosaminoglycanoligosaccharides nor p-nitrophenyl-beta-D-glucuronide were substrates for the enzyme. 2) The molecular weight was found to be about 130,000 by gel filtration, compared with a molecular weight of 280,000-300,000 for beta-glucuronidase, which acts on p-nitro-phenyl-beta-D-glucuronide. 3) The enzyme showed maximal activity at pH 5.0, compared with an optimum pH of 4.5 for beta-glucuronidase, which acts on p-nitro-phenyl-beta-D-glucuronide. 4) The enzyme showed maximal activity in 0.075 M NaCl but no activity above 0.25 M NaCl. 5) The enzyme was inhibited strongly by compounds bearing a sulfate group. 6) The enzyme did not react with an antibody against beta-glucuronidase acting on p-nitrophenyl-D-glucuronide. It is suggested that the enzyme may be involved in the catabolism of glycosaminoglycans, acting especially on chondroitin after the desulfation reaction and/or hyaluronic acid, but showing little involvement with the detoxification system.
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PMID:A new type of exo-beta-glucuronidase acting only on non-sulfated glycosaminoglycans. 210 35

Fish arylsulfatases (arylsulfate sulfohydrolase; EC 3.1.6.1) were resolved into cationic arylsulfatase A-like (ARSA) and anionic arylsulfatase B-like (ARSB) fractions by DEAE-Sephacel chromatography. Green sunfish (GSF) hepatic ARSA was more acidic and more thermostable than bluegill (BG) ARSA. GSF x BG interspecific hybrids preferentially expressed GSF ARSA, while BG x GSF hybrids appeared to produce a dimeric enzyme consisting of both GSF and BG ARSA polypeptides. GSF hepatic beta-glucuronidase (GUS) also proved to be more thermostable than BG GUS. Thermostabilities of GUS produced by reciprocal interspecific hybrids were very similar to that of GSF GUS. Either GSF GUS is preferentially expressed in both interspecific hybrids or both the GSF and BG GUS polypeptides are synthesized in comparable amounts, and the GSF GUS polypeptide sufficiently stabilizes the heterotetramers produced by the hybrids to produce denaturation profiles closely approximating that of the GSF enzyme.
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PMID:Arylsulfatase and beta-glucuronidase expression in green sunfish, bluegill, and their reciprocal interspecific hybrids. 277 68


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