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)

Activities of acid phosphatase, beta-glucuronidase, N-acethyl-beta-D-glucosaminidase and acid beta-galactosidase were investigated histochemically in rabbit corneas. Frozen sections after block fixation in cold 4% formaldehyde with 1% CaCl2 followed by washing in cold physiological saline as well as cold microtome sections of corneas quenched in petroleter chilled with acetone-dry ice mixture, transferred to nonprecooled slides or semipermeable membranes were used. Standard aqueous media were employed in the case of free-floating frozen sections of fixed corneas as well as of cold mictrotome sections (postfixed in cold 4% formaldehyde). Agar media were used in connection with the technic of semipermeable membranes. Gomori method (in the case of acid phosphatase), simultaneous azocoupling methods (substrates derivated of naphthol-AS-BI with hexazonium-p-rosanilin) in the case of acid phosphatase, beta-glucuronidase and N-acetyl-beta-D-glucosaminidase and the indigogenic method in the case of acid beta-galactosidase were applied. Enzyme activities in sections of fixed corneas were minimal in comparison with those in cold microtome sections of unfixed material revealed particularly with the technic of semipermeable membranes which is to be preferred. This technic is recommended in studies concerned with lysosomal enzymes in the cornea, particularly in keratocytes. All enzymes investigated were present in corneal epithelium, keratocytes and endothelium. Acid phosphatase displayed the highest activity followed by beta-glucuronidase and acetyl-beta-D-glucosaminidase. The activity of beta-galactosidase was the lowest. For the demonstration of activities in keratocytes sections parallel to the surface are very suitable. In these sections enzyme activities were demonstrated in small granules (apparently lysosomes) present in the central part of their cytoplasm as well as in projections. Diffuse staining was also seen, being the highest in the case of acid phosphatase.
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PMID:Distribution of acid phosphatase, beta-glucuronidase, n-acetyl-beta-d-glucosaminidase and beta-galactosidase in cornea of albino rabbit. 5 44

Local irradiation of the carotid artery of the hypercholesterolemic rabbit with 2000 rd of X-rays gives rise to infiltration of lipid droplets in the intima and media, becoming visible 3 days after the irradiation. At the same time, acid phosphatase and beta-glucuronidase become activated. These enhanced activities are localized in different cells of the arterial wall. Acid phosphatase activity is localized in the intima, while the beta-glucuronidase activation is found preferentially in the media. A functional heterogeneity of the lysosomal content of the different cells is suggested. A model for the development of the radiation-induced atheromatosis is presented.
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PMID:Initial events in radiation-induced atheromatosis I. Activation of lysosomal enzymes. 12 8

One theory of the development of cleft palate in rats involves the action of lysosomal enzymes secreted by epithelial cells at the time of fusion of the palatal shelves. To test this theory we studied the biochemistry of the palates of fetal rats daily between days 14 and 19 (from 3 days before to 3 days after palate closure). Triamcinolone was administered once im on gestation day 14 to Wistar rats; 0.5 mg/kg body weight produced approximately 50% cleft palates. Pooled control palatal tissue was compared with pooled experimental tissue; that from fetuses with clefts being pooled separately from those not affected. Acid phosphatase and beta-glucuronidase were assayed. Concentration vs. time curves for both enzymes were very similar. Prior to the time of palate closure both enzymes were present in low concentration. Between days 16 and 17, the normal time of closure, there was an abrupt increased in enzyme concentration, with experimental tissue showing a significant elevation over control tissue on days 17 and 18. Alkaline phosphatase was also present in small amounts before closure and significantly higher in control tissue on day 17. Protein was depressed in palates having clefts on day 17; thus the ratio of enzyme activities to protein synthesis was significantly elevated at a critical time. Unaffected experimental palates had a normal ratio. These results suggest imbalanced acid phosphatase, beta-glucuronidase, and alkaline phosphatase activity compared with protein synthesis at the time of palate closure following triamcinolone in rats.
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PMID:Tissue phosphatase changes following triamcinolone associated with cleft palate in rats. 16 57

The histochemistry of the hepatic parenchymal cells was studied in four Callithrix jacchus. A large amount of glycogen was noted throughout the lobules while the UDPG-GT and the phosphorylases were found unevenly distributed by the hepatic strands with different degrees of reactivity. Near the central vein one of the livers showed PAS-positive nuclear corpuscles that were more conspicuous in the hepatic cells with a larger amount of cytoplasmic glycogen and weaker UDPG-GT and phosphorylase reactivities. G-6PA (in a larger amount) and LDH (in a moderate amount) were found evenly distributed in the hepatic strands. F-1-6PA was seen sometimes with a stronger reactivity at the peripheral part of the lobules. The enzymes of the pentose shunt (G-6PDH, 6-PGDH and NADPH-2-TR) reacted strongly and as a rule evenly distributed near the hepatic lobules. Occasionally they reacted more intensely in the row of hepatic cells disposed just around the central vein. Cytochrome oxidase showed a very faint reaction. Cis-aconitase and ICDH were weak or moderate. NADH-2-TR more than SDH more than MDH were seen frequently diffused near the hepatic strands. SDH and MDH in some instances showed a stronger reactivity in the row or group of hepatic cells around the central vein. ATPase at pH 6.3 was negative in the marmoset liver; ATPase at pH 7.4 was mainly found in the wall of the portal area vessels; ATPase at pH 8.5 showed a stronger reactivity in the cytoplasm of the hepatic cells and ATPase at pH 9.4 was more abundant in the bile capillaries. The reactivity of the lipid metabolism enzymes was moderate with regard to alpha-GPDH or negligible with regard to beta-OHBDH. Acid phosphatase showed a stronger reaction, but almost limited to the Kupffer cells. The hepatic cells showed only a moderate amount of RNA. Some enzymes of the protein metabolism, such as GDH and leucine aminopeptidase showed a stronger reactivity while some others, such as alanyl aminopeptidase and MAO, were seen diffused near the hepatic lobules in a small amount. Enzymes of the mucopolysaccharide metabolism were not found at all (beta-glucuronidase) or showed only a weak reactivity, such as xylitol dehydrogenase.
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PMID:Histochemical data on the liver of the marmoset (Callithrix jacchus). 16 44

1. The injection into mice of a single dose of conduritol B epoxide, a covalent inhibitor of glucosidases, quickly produced changes in tissue levels of beta-D-glucuronidase (EC 3.2.1.31). The specific activity of the enzyme decreased in liver, spleen and kidney while brain showed little change. The inhibitor did not act on glucuronidase in vitro, so the effect of the inhibitor is complex, possibly a result of the loss of glucosidase activity. Since glucuronidase contains glucose, we suggest that the transport of the enzyme between subcellular regions and tissues involves loss of part of the glucose moieties. 2. Levels of glucocerebrosidase (D-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45) dropped very rapidly after epoxide injection, reaching a minimum at 1 h in liver. There was a noticeable restoration of activity within the next 1--2 h. Aryl beta-glucosidase (EC 3.2.1.21) decrease somewhat less than cerebrosidase, reaching a minimum within 2 h. It too showed some recovery of activity within 3 h. 3. Acid phosphatase rose slightly in liver but not in brain. alpha-L-Fucosidase and angiotensin-converting enzyme were not affected by the epoxide injection. The latter two enzymes are known to contain glucose. 4. Injection of a hemolyzing agent, phenylhydrazine, produced an increased level of glucuronidase in liver and spleen within 6 days, but not in kidney. This enhancement was a little less in mice previously injected with the glucosidase inhibitor. 5. Mice injected with the epoxide once a day eight times showed a distinct rise in brain glucuronidase level, as well as a rise in brain weight. However, the other organs showed only the same decrease in glucuronidase specific activity noted with the single injection protocol. It is suggested that the difference is due to the blood-brain barrier, which could slow the loss of brain glucuronidase from the extracellular fluid.
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PMID:Enzymic effects of beta-glucosidase destruction in mice. Changes in glucuronidase levels. 21 40

Isoelectric focusing was used to study the multiple forms of acid phosphatase, arylsulfatase, beta-glucuronidase and beta-N-acetylhexosaminidase in lysosomes isolated from rat kidney. The isoelectric points of the main protein and hydrolase peaks were 1-1.5 units lower when electrofocusing was done in a pH 3-10 gradient than in a pH 10-3 gradient, apparently because the lysosomal constituents aggregated strongly at their isoelectric points and tended to settle somewhat in the gradient due to gravity. In the extended pH gradient the acidic form of each hydrolase occurred as asingle, relatively discrete peak. However, when pooled acidic fractions were refocused in a restricted pH gradient (pH 6-3 or 3-5) multiple acidic enzyme and protein components were resolved with isoelectric points between 2.7 and 5.1. When autolysis was minimized by extracting lysosomal fractions at alkaline pH (0.2% Triton X-100, 0.1%p-nitrophenyloxamic acid, 0.1 M glycine buffer, pH9) and including 0.1%p-NITROPHENYLOXAMIC ACID, AN INHIBITOR OF LYSOSOMAL NEURAMINIDASE AND CATHEPSIN D, in the pH gradient, arylsulfatase, beta-glucuronidase and beta-N-acetylhexosaminidase occurred in two forms, an acidic form with an isoelectric point of about 4.4, and a basic form with an isoelectric point close to 6.2, 6.7 and 8.0, respectively. Acid phosphatase occurred in three forms with isoelectric points of 4.1, 5.6 and 7.4. When some autolytic digestion was permitted by extracting lysosomal fractions in an acidic medium (0.2% Triton X-100, 0.1 M sodium acetate buffer, pH 5.2) AT 0-4DEGREES C and omitting p-nitrophenyloxamic acid from the gradient, the acidic form of beta-glucuronidase and the intermediate form of acid phosphatase were lost, the isoelectric points of the acidic forms of acid phosphatase, arylsulfatase and beta-N-acetylhexosaminidase were increased 0.6-1.2 units, and the isoelectric point of the basic forms of acid phosphatase, arylsulfatase and beta-glucuronidase was increased 0.5 unit. When lysosomal extracts were incubated with bacterial neuraminidase before electrofocusing, the acidic forms of acid phosphatase, arylsulfatase and beta-glucuronidase were largely lost, the isoelectric point of the acidic form of beta-N-acetylhexosaminidase was increased from 4.5 to 6.4, and the isoelectric points of the basic forms of all four hydrolases were increased 0.5-1.5 units. Autoincubation of lysosomal extracts in vitro at pH 5.2 PRODUCED SIMILAR, THOUGH LESS MARKED, effects. cont'd
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PMID:Isoelectric-focusing behavior of acid hydrolases in rat kidney lysosomes. Effects of the pH gradient, autolysis and neuraminidase. 23 55

Isoelectric focusing was used to investigate the multiple forms of acid phosphatase, arylsulfatase, beta-glucuronidase, beta-galactosidase and beta-N-acetylhexosaminidase in the following, previously characterized subcellular fractions from rat kidney: a special rough microsomal fraction, enriched up to 9-fold over the homogenate in acid hydrolases; a smooth microsomal fraction; a Golgi membrane fraction enriched about 2.5-fold in acid hydrolases and 10- to 20-fold in several glycosyl transferases; and a lysosomal fraction enriched up to 25-fold in acid hydrolases. The electro-focusing behavior of the hydrolases in these fractions was markedly sensitive to the autolytic changes that occur under acidic conditions, even at 4 degrees C. Autolysis was minimized by extracting fractions in an alkaline medium (0.2% Triton X-100, 0.1 M sodium glycinate buffer, pH 10, 0.1 % p-nitrophenyloxamic acid) and adding p-nitrophenyloxamic acid (0.1 %), AN INHIBITOR OF LYSOSOMAL NEURAMINIDASE AND cathepsin D, to the pH gradient. The enzymes in the lysosomal fraction displayed a characteristic bimodal or trimodal distribution. Arylsulfatase, beta-glucuronidase and beta-N-acetylhexosaminidase occurred in an acidic form with an isoelectric point of 4.4, and a basic form with an isoelectric point of 6.2, 6.7 and 8.0, respectively. Acid phosphatase and beta-galactosidase occurred in an acidic, intermediate and basic form with isoelectric points of about 4. 1, 5.6 and 7.4, respectively. In the special rough microsomal fraction these enzymes were mostly in a basic form with isoelectric points between 7.5 and 9; these were 1-2 units higher than the corresponding basic forms in the lysosomal fraction. Treatment of extracts of the rough microsomal fraction with bacterial neuraminidase raised the isoelectric points of all five hydrolases by 1-2.5 units, indicating the presence of some N-acetylneuraminic acid residues in these basic glycoenzymes. The hydrolases in the Golgi fraction were largely in an acidic form with isoelectric points similar to or lower than those of the corresponding acidic components in the lysosomal fraction. The hydrolases in the smooth microsomal fraction showed isoelectric-focusing patterns intermediate between those in the rough microsomal and the Golgi fractions. These findings support the following scheme for the synthesis, transport and packaging of the lysosomal enzymes. Each hydrolase is synthesized in a restricted portion of the r
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PMID:Changes in electronegativity of lysosomal hydrolases during intracellular transport. An isoelectric-focusing study in subcellular fractions of rat kidney. 23 56

The activities of acid phosphatase, beta-glucuronidase, beta-galactosidase, and N-acetyl-beta-D-glucosaminidase were investigated in the normal rabbit cornea. For all spectrophotometric assays, appropriate p-nitrophenyl derivates were used. Only beta-glucuronidase were determined employing phenolphthalein glucuronid as a substrante. Acid phosphatase revealed the highest activity, followed by N-acetyl-beta-D-glucosaminidase and beta-galactosidase. In the case of beta-glucuronidase the lowest activity was found. The results on the rabbit cornea are compared with those on some other tissues described in the literature. Correlation of biochemical data and histochemical findings in the same species is briefly discussed.
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PMID:Biochemical study on some acid hydrolases in the normal rabbit cornea. 30 56

The human peripheral blood lymphocytes are characterized by different surface markers: The B lymphocytes by the EAC rosettes and surface immunoglobulin and the T lymphocytes by the E-rosettes. Each lymphoid population has been studied for cytochemical parameters (Acid phosphatase, beta-glucuronidase) by light microscopy and for ultrastructural characteristics by micromanipulation and immunoelectronmicroscopy. It has been shown that the studied enzymes are markers for T cells with high affinity for sheep red blood cells and that the separation of lymphocytes by the rosette techniques leads to homogenous cell populations at the ultrastructural level. A classification of peripheral lymphocytes according to their immunocytochemical profile is discussed.
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PMID:Cytochemical and ultrastructural characters of human peripheral blood lymphocytes according to their surface markers. 31 99

The cytochemical profiles of B and T lymphocytes from the bloods of eight normal donors and the tonsils of three normal individuals were studied. An intense and localized alpha-naphthyl acetate esterase (alpha-NAE) activity was found in the majority of blood and tonsillar T lymphcytes, in contrast to the very low alpha-NAE activity observed in the blood and tonsillar B lymphocytes. A very low percentage of tonsillar B lymphocytes had beta-glucuronidase (betaG) activity, while relatively normal betaG activity was observed in the tonsillar T lymphocytes and the blood B and T lymphocytes. Acid phosphatase (AcP) activities were found to be similar in both B and T lymphocytes from blood and tonsils. These findings suggest that the alpha-NAE reaction may be useful as a cytochemical marker for distinguished B from T lymphocytic proliferations. They also revealed that there is no appreciable difference in AcP and betaG activity between B and T lymphocytes obtained from the blood of normal donors.
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PMID:Cytochemical findings in human nonneoplastic blood and tonsillar B and T lymphocytes. 34 98


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