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)

Cultured normal human articular cartilage chondrocytes exhibited decreasing levels of arylsulfatase A and B activities when grown in the presence of increasing levels of ascorbic acid (0 to 90 mug/ml) in the media. That this was not a general effect on all lysosomal enzymes was supported by the increase in acid phosphatase activity and no change in beta-glucuronidase activity observed with increasing levels of vitamin C under identical culture conditions. No decrease in either arylsulfatase activity was observed when ascorbic acid was replaced by ascorbate-2-sulfate. Ascorbic acid did not inhibit either arylsulfatase activity when added directly to the assay mixture. These data, combined with results of mixing experiments, suggest that the effect of vitamin C is mediated through cellular factors produced in response to its inclusion in the growth media.
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PMID:Effect of ascorbic acid on arylsulfatase A and B activities in human chondrocyte cultures. 1 Oct 78

Sodium sulfate increases the hydrolysis of urinary 17-hydroxycorticosteroid glucuronides with beta-glucuronidase preparations derived from Helix pomatia because it removes the inhibitory activity of urinary high-molecular-weight substances. For maximum hydrolysis of urinary 17-hydroxycorticosteroid glucuronides, the hydrolysis [5 ml of urine, 0.5 ml of 2 mol/liter acetate buffer (pH 5.0)] should be conducted in the presence of sodium sulfate (final concentration: 80 g/liter) with (a) 600 Fishman units of the enzyme per milliliter of urine (18 h at 52 degrees C) or (b) with 1500 units of the enzyme per milliliter of urine (3 h at 57 degrees C). Under conditions a, analytical recovery of steroid glucuronides added to 12 urine samples was 99 +/- 2.1% (96-102%). Values obtained for 20 urine samples with this method were 99 +/- 2.7% (93-104%) as great as those yielded by a method in which 600 units of the enzyme from bovine liver are used together with sodium sulfate (18 h at 48 degrees C).
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PMID:Improved hydrolysis of urinary 17-hydroxycorticosteroid glucuronides with beta-glucuronidase from Helix pomatia, on adding sodium sulfate. 2 63

Change in beta-glucuronidase activity of six Yoshida ascites hepatomas was examined after treatment of host rats with one of 12 anticancer agents. The hepatomas, AH-66F, AH-130, AH-109A, AH-60C, and AH-44, in decreasing order showed more or less distinct increase in beta-glucuronidase activity after treatment of the rats with Nitromin, Endoxan, 864-T, Carbazilquinone, Mitomycin-C, Toyomycin, Daunomycin, Neocarzinostatin, vincristine sulfate, 5-fluorouracil, or cytosine arabinoside only when the cytological effect was positive. Moreover, degree of the increase was generally correlated with that of cytological effect. Bleomycin was ineffective either enzymically or cytologically. AH-66 was insensitive to any of the agents tested in increasing beta-glucuronidase activity and showed only a very slight cytological response to some of the agents. Acid deoxyribonuclease behaved like beta-glucuronidase but to a lesser extent. The above order of drug sensitivity of the hepatomas was not in parallel with that of normal beta-glucuronidase level, which also did not correlate with the life span of host rats.
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PMID:Beta-glucuronidase activity of Yoshida ascites hepatomas of different drug-sensitivity and its change after treatment of host rats with various anticancer agents. 5 96

We have purified beta-galactosidase and beta-glucuronidase from macrophages of thioglycollate-treated mice using concanavalin A chromatography and immunoprecipitation. The apparent molecular weight of the beta-galactosidase subunit, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, changed during a long term pulse-chase experiment. Following a 1-h pulse with [3H]leucine, radiolabel was present exclusively in an Mr = 82,000 form. However, after a 3-h chase in medium containing unlabeled leucine, most label migrated at Mr = 63,000, and at 24 h, all label was in the Mr = 63,000 form. Electrophoresis of peptides produced by cyanogen bromide cleavage of immunoprecipitates demonstrated structural similarities between precursor and mature forms. A mutation in the mouse, which is known to depress the rate of synthesis of beta-galactosidase in many cell types, proportionately decreased incorporation of [3H]leucine into both the Mr = 82,000 and 63,000 forms. Therefore, by kinetic, structural, and genetic evidence, the large molecular weight beta-galactosidase is a precursor of mature macrophage enzyme. No precursor of the Mr = 75,000 subunit of beta-glucuronidase was detected.
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PMID:Biosynthesis of two lysosomal enzymes in macrophages. Evidence for a precursor of beta-galactosidase. 11 27

The formation of glutathione (GSH) conjugate in the detoxification of [1-14C]-naphthalene and [naphthyl-14C]-carbaryl was investigated using rat liver homogenate. The mercapturic acid conjugate in rats was also investigated by collection of urine after intraperitoneal injection of 14C substrates. The formation of water-soluble metabolites in vitro from naphthalene was dependent on the amount of glutathione added, but this was not seen in carbaryl metabolism. In vitro, the metabolism of [1-14C]-naphthalene produced 50% GSH conjugates in the incubation mixture, whereas in vivo the metabolism of this compound produced 65% mercapturic acid conjugate in the urine. There was no evidence of GSH or mercapturic acid conjugate in the metabolism of [naphthyl-14C]-carbaryl in vitro and in vivo. This conclusion was made by comparing the nature and chemical characteristics of GSH and mercapturic acid conjugates formed in [1-14C]-naphthalene metabolism. With the aid of the specific enzyme (e.g. beta-glucuronidase and sulfatase) and acid hydrolysis, the water-soluble metabolites of [naphthyl-14C]-carbaryl were tentatively recognized as glucuronide or sulfate conjugated mainly with 5,6-dihydro-5,6-dihydroxycarbaryl or N-hydroxy-methyl carbaryl and their hydrolytic products. This data demonstrated that the substituent group on the naphthalene molecule may affect the significance of GSH conjugation.
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PMID:Glutathione and mercapturic acid conjugations in the metabolism of naphthalene and 1-naphthyl N-methylcarbamate (carbaryl). 12 Feb 42

Four different methods of isolation and purification were utilized to study steroids in urine of male newborns which was collected during the first 5 days of life. These methods included celite column, ion exchange column and thin-layer chromatography, solvolysis and enzyme hydrolysis with beta-glucuronidase and aryl sulfatase. Procedural losses were evaluated by using radioactive internal standards. Final quantitation of each steroid was achieved by comparison of its chromatographic and quantitative behavior with the respective standard steroids on various gas-liquid chromatography systems, either as parent compound or as trimethylsilyl ether derivative. The following steroids were found in the amounts indicated: progesterone, 2.1 mug/1 (pool I), 4.6 mug/1 (pool III); pregnanediol, 625.0 mug/1 (pool IIa), 605.0 mug/1 (pool IIb glucuronide), 25.4 mug/1 (pool IIb sulfate), 4.2 mug/1 (pool IIb free), 729.0 mug/1 (pool III); 16alpha-hydroxyprogesterone, 713.0 mug/1 (pool III), 16alpha-hydroxypregnenolone, 14,000.0 mug/1 (pool III); 16alpha-hydroxydehydroepiandrosterone, 2,350.0 mug/1 (pool III); 16-dehydroprogesterone, 155.0 mug/1 (pool I), 21.2 mug/1 (pool IIb glucuronide), 97.5 mug/1 (pool IIb sulfate), 5.3 mug/1 (pool III); 16-dehydropregnenolone, 382.0 mug/1 (pool I), 1,380 mug/1 (pool IIb glucuronide), 172.0 mug/1 (pool IIb sulfate), 174.0 mug/1 (pool III); 16-dehydropregnanolone, 8.3 mug/1 (pool I), 239.0 mug/1 (pool IIb sulfate). Pregnenolone, pregnanolone, 17alpha-hydroxyprogesterone and 17alpha-hydroxypregnenolone could not be detected. The results support the concept that the steroid patterns of urine of the newborn and amniotic fluid are very similar and that the amniotic fluid steroid content is mainly dependent on fetal urinary steroid excretion. The data on delta16-C21-steroids are discussed.
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PMID:Studies on steroids in urine of the male newborn. 12 3

The polysaccharide from blackgram (Phaseolus mungo) has been previously reported to cause lower cholesterol, phospholipids and triglyceride levels in rats fed either low-or high-fat diets containing cholesterol. The effect of this polysaccharide fraction as compared to that of glucose and sucrose on the metabolism of glycosaminoglycans and glycoprotein has been studied. The pattern of change in the levels of different glycosaminoglycans varied in the different tissues. Sucrose fed animals gave lower levels of sulphated glycosaminoglycans in the aorta and liver. The polysaccharide and glucose fed animals gave comparable values in the aorta except in the case of chondroitin sulfate B which was higher and heparin lower in the polysaccharide group. L-glutamine:D-fructose-6-phosphate amino transferase and UDPG dehydrogenase were lowest in the sucrose fed animals and highest in the polysacchride group with the animals in the glucose group showing intermediate values, but UDPG pyrophosphorylase, while highest in the polysaccharide group, was similar in the glucose and sucrose groups. Some of the degrading enzymes studied-beta-glucuronidase, hyaluronidase and aryl sulphatase-were highest in the sucrose group and generally lowest in the polysaccharide group. Levels of 3'-phosphoadenosine-5'-phosphosulphate, the biological sulphating agent, the sulphate activating system which includes ATP sulphurylase and APS kinase and sulphotransferase activity were also lowest in the sucrose fed group and highest in the polysaccharide group. The glycoprotein concentration was highest in the liver and lowest in the kidney in the sucrose group.
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PMID:Nature of the dietary carbohydrate and metabolism of glycosaminoglycans and glycoproteins in rats. 17 34

Rat preputial gland beta-glucuronidase [ED 3.2.1.31] was purified by ammonium sulfate precipitation, ethanol fractionation, gel filtration on Sephadex G-200 and crystallization. The purified enzyme appeared homogeneous on electrophoresis in polyacrylamide gel, and on analytical ultracentrifugation and had a molecular weight of approximately 320,000, and a sedimentation coefficient of 12S. SDS polyacrylamide gel electrophoresis indicated that the enzyme consisted of subunits with molecular weight of 79,000, so the native enzyme appeared to be a tetramer. The Km with p-nitrophenyl beta-D-glucosiduronic acid as substrate was about 0.53 mM. The enzyme had a single pH optimum at 4.5. The enzyme had a very low content of sulphur-containing amino acid and contained 5.7 per cent carbohydrate, consisting of mannose, glucose, fucose, galactose, and glucosamine in a ratio of 44;9;6;2;41. Sialic acid was not detected in the crystallized enzyme.
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PMID:Beta-glucuronidase of rat preputial gland. Crystallization, properties, carbohydrate composition, and subunits. 23 93

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

Biochemical studies are presented on two siblings with some features of Mucolipidosis III, but with distinctive clinical findings. Levels of beta-galatosidase, alpha-mannosidase, beta-glucuronidase, N-acetyl-beta-glucosaminidase and alpha-fucosidase found in serum from these patients ranged from 10 to 10 times higher than normal. The ratio of heat stable to heat labile serum isoenzymes of N-acetyl-beta-glucosaminidase is considerably greater than normal. An extremely low activity of beta-galactosidase was found in fibroblasts cultured from one patient. Levels of the remaining enzymes were in the low normal range. Similarly, beta-galactosidase levels were low in heart, kidney, liver, spleen and lung of one patient who died during the course of the study. Activities of the remaining enzymes were close to normal. No excessive excretion of mucopolysaccharide was noted, however, changes in distribution of several fractions were found. Mucopolysaccharide labeled with radioactive sulfate was degraded by cultured fibroblasts at a normal rate. In addition to clinical differences, the biochemical studies further demonstrate the uniqueness of these patients.
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PMID:A new variant mucolipidosis: biochemical investigations on two siblings. 41 May 66


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