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)

Sera from 9 persons with either biopsy-proven alcoholic liver disease or a history of chronic, excessive ethanol consumption were analyzed for their content of various hydrolases. Compared to controls, significant elevations in the following enzyme activities were seen in sera from the patient population: acid phosphatase (2.0-fold), beta-glucuronidase (2.1-fold), hexosaminidase (1.4-fold), and alpha-L-fucosidase (2.3-fold). In addition, alpha-mannosidase activity, previously reported to be unchanged in cases of hepatic cirrhosis [Reglero et al., Clinica chim. Acta 130: 155-158], (1980) was found to be significantly increased (p less than 0.001) when assays were performed at acid (pH 4.5) or intermediate (pH 5.5) hydrogen ion concentrations. Fractionation of sera on DEAE-Sephadex columns showed that the increase in alpha-mannosidase activity in the serum of patients with alcoholic liver disease was due to increases in the level of at least one 'acid alpha-mannosidase' and two intermediate pH optimum alpha-mannosidases. The general increase in the activity of a group of glycosidases is consistent with a hypothesis involving decreased clearance of glycoproteins from the blood of persons with hepatic cirrhosis.
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PMID:Serum alpha-mannosidase in patients with alcoholic liver disease. 671 94

We have isolated from monkey (Macaca radiata) brain lysosomal fraction by phosphomannan-Sepharose chromatography a protein that binds four different lysosomal enzymes, beta-hexosaminidase, beta-glucuronidase, alpha-L-fucosidase and arylsulfatase. The isolated protein which appeared in an aggregated homogeneous form on gel electrophoresis under non-denaturing conditions at both pH 8.3 and pH 5.0 was found to be heterogeneous on SDS-gel electrophoresis with molecular weights less than 67,000. Binding was partly abolished by periodate treatment or by alkaline phosphatase treatment of the lysosomal enzymes. Binding was completely abolished by pronase digestion of the binding protein. Of the different sugars tested for inhibition of binding, mannose-6-phosphate was most effective followed by mannose and N-acetyl glucosamine while glucose and fucose were ineffective.
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PMID:A binding protein for lysosomal enzymes isolated from brain by phosphomannan-sepharose chromatography. 684 56

The activities of 21 enzymes (belonging to four classes of enzymes) involved in different metabolic pathways were assayed in blood sera of healthy young and adult/elderly groups of humans, rats and pigs, to determine whether activity changes coinciding with changes in age and aging could be detected. In all three species analysed, measurable activities (performed by highly specific and sensitive techniques, generally spectrofluorimetric procedures) were found, usually following a decreasing order of: among glycosidases, beta-N-acetylglucosaminidase (NAG) > alpha-L-fucosidase > alpha-mannosidase > beta-glucuronidase > beta-galactosidase > alpha-galactosidase. In addition, among esterases very high values were found for arylesterase and acid phosphatase. By contrast, no measurable activity was found for the remaining enzymes assayed (8 hydrolases, 1 oxidoreductase, 3 transferases and 1 lyase). In the elderly group of humans, significantly higher activities (P < or = 0.05) were found for NAG, alpha-mannosidase and beta-glucuronidase in comparison to the adult and young groups. However, several activities in rats and all activities in pigs decreased with age. In conclusion, differences in the activities of 6 lysosomal glycosidases and 2 esterases (but no significant differences for another 13 enzymes belonging to several enzyme classes) are found in the sera of healthy humans, rats and pigs. These differences coincide with changes observed in aging.
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PMID:Evaluation of the activities of eight lysosomal hydrolases in sera of humans, rats and pigs of different ages. 948 85


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