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:3.2.1.21 (beta-glucosidase)
3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The optimal reaction conditions and kinetic properties of eleven leukocyte acid hydrolases determined with the use of fluorigenic derivatives of 4-methyl-umbelliferone are described. The enzymes studied were acid phosphatase, aryl sulfatase, alpha- and beta-glucosidase, alpha- and beta-galactosidase, alpha-mannosidase, N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucuronidase and alpha-fucosidase. More than 90% of the activity of each enzyme was released into a 27,000 X g supernatant by a double sonication procedure employing 0.9% sodium chloride and 0.1% Triton X-100. The Km values obtained were similar to those previously reported for chromogenic subtrates. A single Km value could not be derived for beta-galactosidase because its double reciprocal plot was not linear. All enzymes could be measured with less than 10 mug of protein within 15 min. Activators and inhibitors studied included the chloride salts of Na+, K+, Zn2+, Ca2+, Mg2+, Hg2+, and Fe2+ as well as p-chloromercuriphenysulfonate, glutathione, BAL, EDTA, EGTA, Triton X-100 and sodium taurocholate. The reaction conditions described in this report can be used for the diagnosis of various lysosomal storage diseases and should facilitate the development of automated procedures for the analysis of these eleven enzyme activities with small quantities of blood.
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PMID:Human leukocyte acid hydrolases: characterization of eleven lysosomal enzymes and study of reaction conditions for their automated analysis. 0 26

Serum enzymes have not proved useful in evaluation of patients with early colon cancer, but certain enzymes such as transpeptidase, phosphohexone isosomerase, or 5'-nucleotidase have been of assistance in following the course of the disease, particularly in patients with metastatic spread to the liver. Attempts have been made to improve the utility of enzyme analysis in colon cancer by examination of enzyme patterns in colon biopsy specimens, feces, and colon washings. These studies, which will be summarized, are of importance in the possible development of diagnostic tools and as probes in the understanding of the etiology of colon cancer. The technical problems in carrying out these assays in humans, as well as the significance of the activity of aryl sulfatase, beta-glucuronidase, beta-glucosidase, lactic dehydrogenase, glucose-6-p-osphate dehydrogenase, and other enzymes will be considered.
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PMID:Enzymes in colon cancer. General information. 76 57

Enhanced chemiluminescent assays for hydrolase enzymes have been developed using proenhancer and pro-anti-enhancer substrates. Alkaline phosphatase is measured using disodium para-iodophenyl phosphate (proenhancer) which is converted to para-iodophenol and this in turn enhances the light emission from the horseradish peroxidase catalysed chemiluminescent oxidation of luminol by peroxide. An alternative strategy uses para-nitrophenyl phosphate which is converted by alkaline phosphatase to para-nitrophenol which inhibits the enhanced chemiluminescent reaction. The detection limit for the enzyme using the proenhancer and pro-anti-enhancer assays was 100 attomoles and 1 picomole, respectively. The proenhancer strategy was effective in assays for beta-D-galactosidase, beta-D-glucosidase and aryl sulfatase. A limited comparison of the proenhancer and a conventional colorimetric assay for an alkaline phosphatase label in an enzyme immunoassay for alpha-fetoprotein showed good agreement.
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PMID:Chemiluminescent assay of enzymes using proenhancers and pro-anti-enhancers. 172 39

Male Wistar rats received a low-protein (4.5% protein) diet during 30 days, and T-2-toxin was administered to them through a gastric tube, in a dose of 0.54 mg/kg, during 15 days. The results obtained showed activation of hepatic lysosomal enzymes (sulfatase A and B aryl and beta-glucosidase) and alkaline phosphatase, and to an essential suppression of enzymatic activity of peroxisomes - catalase, glycolate oxidase and D-amino acid oxidase. A sharp aggravation of the intoxication symptoms and pronounced intensification of changes in enzymatic activity in the liver, spleen, thymus and blood serum were recorded in the animals given T-2 toxin simultaneously with the low-protein diet.
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PMID:[Enzyme parameters in the evaluation of the combined effects of protein deficiency and T-2 mycotoxin]. 289 95

Soybean plants were grown for 90 days and spinach plants for 64 days in a mixture of sterilized greenhouse soil and sand containing 10 ppm pentachlorophenol. All plant parts and soil samples were extracted and separated into nonpolar and polar fractions. Major nonpolar and polar metabolites were identified by gas-liquid chromatography and mass spectrometry. Nonpolar fractions from both soybean and spinach plants were found to contain pentachlorophenol and its metabolites, 2,3,4,6-tetrachlorophenol, methoxytetrachlorophenol, 2,3,4,6-tetrachloroanisole, and pentachloroanisole. Cleavage of polar metabolites from the soybean plants by acid hydrolysis yielded organic solvent-extractable products. These products were identified as pentachlorophenol, 2,3,4,6-tetrachlorophenol, and methoxytetrachlorophenol. Cleavage of polar materials from spinach plants yielded only pentachlorophenol. The polar metabolites from the soybean plants were also subjected to enzymatic cleavage by beta-glucosidase. The conjugates consisted mostly of O-glucosides of the same metabolites released by acid hydrolysis. Failure of hydrolysis by aryl sulfatase indicated that very little or no sulfates were present. The metabolites found in the plants were not detected in soil samples obtained from pots immediately after the plants were harvested.
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PMID:Uptake, translocation, and transformation of pentachlorophenol in soybean and spinach plants. 403 60

Toxicity tests on Culex pipiens fatigans with propoxur (o-isopropoxyphenyl methylcarbamate) and carbofuran (2,2-dimethyl-2,3-dihydrobenzofuranyl-7-methylcarbamate) indicated that both compounds are fast-acting insecticides. Transfer of treated larvae to fresh water results in their partial recovery from knockdown.Propoxur is metabolized by resistant and susceptible larvae by their homogenate-reduced nicotinamide-adenine dinucleotide phosphate (NADPH(2)) enzyme system and by the microsome-plus-soluble fraction of mouse-liver extracts to at least 10 organosoluble metabolites with the isopropoxy group intact. The major metabolites, which are primarily hydroxylation products or the result of degradation of these products, have tentatively been identified as: acetone plus o-hydroxyphenyl methylcarbamate, 2-isopropoxy-5-hydroxyphenyl methylcarbamate, 2-isopropoxyphenyl carbamate, and 2-isopropoxyphenyl N-hydroxymethylcarbamate. Upon incubation of water-soluble products from treated larvae with beta-glucosidase, beta-glucuronidase, aryl sulfatase and acid phosphatase, the conjugates are hydrolysed, liberating mainly hydroxylated carbamates.The results indicate that slower absorption as well as faster detoxification by hydroxylation mechanisms, together with conjugation with polar molecules and elimination, are major factors in resistance of mosquito larvae to substituted-aryl methylcarbamate insecticides.
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PMID:Carbamate resistance in mosquitos. The metabolism of propoxur by susceptible and resistant larvae of Culex pipiens fatigans. 531 55

Sphingolipidoses are an heterogeneous group of inherited disorders of lipid metabolism affecting primarily the central nervous system. These disorders occur chiefly in the pediatric population, and the degenerative nature of the disease processes is generally characterized by diffuse and progressive involvement of neurones (gray matter) with psychomotor retardation and myoclonus or of fiber tracts (white matter) with weakness and spasticity. Biochemical research has identified the defects in the sphingolipidoses to specific lysosomal enzymes. For example, Niemann-Pick disease lacks sphingomyelinase; Krabbe's disease lacks galactocerebrosidase; Gaucher's disease lacks beta-D-glucosidase; metachromatic leukodystrophy lacks sulfatase; Tay-Sachs disease lacks hexosaminidase A; and generalized gangliosidosis lacks beta-galactosidase. Although there are no currently available modes of rendering corrective therapy in these disorders, a definitive diagnosis is possible both antepartum as well as postpartum. This information provides a sound and accurate basis for genetic counseling.
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PMID:Sphingolipidoses. 555 2

A heat-stable protein was isolated from the spleen of a patient with Gaucher's disease. This protein will activate glucosylceramide beta-glucosidase activity (Ho, M.W. and O'Brien, J.S. (1971) Proc. Natl. Acad. Sci. U.S.A. 68, 2810-2813). When the specificity of this activator was tested using other enzymes and substrates, it was found to activate galactosylceramide beta-galactosidase activity and sphingomyelinase but not GM1 beta-galactosidase or sulfatide sulfatase. The ability to stimulate galactosylceramide beta-galactosidase was optimum at pH 4.6 in the presence of pure phosphatidylserine or other acidic lipids such as sulfatide and phosphatidylinositol. The partially purified activator protein could stimulate galactosylceramide beta-galactosidase activity in brain, liver, leukocytes and cultured fibroblasts. It was not able to stimulate the activity of this enzyme in tissue samples from patients with Krabbe's disease, demonstrating that it was acting on galactosylceramide beta-galactosidase and not GM1 beta-galactosidase. It was slowly denatured by treatment with Pronase, reaching 16% of starting levels after 24 h at 50 degrees C. Attempts to separate the abilities of this activator preparation to stimulate several lysosomal hydrolases by column chromatography were not successful.
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PMID:A protein activator of galactosylceramide beta-galactosidase. 712 30

The purpose of the present study was to determine the role of cardiac lysosomal enzymes in the pathogenesis of the cardiomyopathy that develops in the genetically diabetic C57BL/KsJ db+/db+ mice. Db+/db+ mice and littermate controls were sacrificed as age-matched pairs between 5 and 26 weeks of age. C57BL/6J ob/ob mice and littermates served as other controls. Following anesthesia, the hearts were excised, homogenized, and the following enzymatic activities measured: N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucosaminidase, aryl sulfatase, alpha-mannosidase, alpha-glucosidase, beta-galactosidase, beta-glucosidase, total rho-nitrophenyl phosphatase, acid phosphatase. and 5'-phosphodiesterase type IV. There is a progressive decrease in cardiac lysosomal enzyme activities of db+/db+ mice for the period 5 to 21 weeks of age. All enzyme activity is depressed significantly during the 9- to 21-week interval: alpha-glucosidase, beta-glucosidase, alpha-mannosidase, beta-galactosidase, acid phosphatase, N-acetyl-beta-galactosaminidase, 5'-phosphodiesterase type IV, and total rho-nitrophenyl phosphatase are reduced approximately 10 to 20 per cent, whereas beta-glucosaminidase, aryl sulfatase, and N-acetyl-beta-glucosaminidase are decreased almost 40 to 50 per cent. In contrast, cardiac lysosomal enzymic activity in the ob/ob mice does not differ significantly from controls aside from aryl sulfatase (20 per cent decrease) and beta-glucosidase (10 per cent decrease). This decrease in lysosomal enzyme activity can explain the accumulation of large residual bodies and interstitial material that occurs in the myocardium of the db+/db+ animals as part of the cardiomyopathy.
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PMID:Lysosomal enzymes in the heart of the genetically diabetic mouse. 742 Nov 26

Prosaposin contains separate domains in tandem for four saposins, A, B, C, and D. These mature saposins are produced by limited proteolysis of prosaposin. They are involved in lysosomal hydrolysis of GM1 ganglioside, gluco- and galactocerebrosides, sulfatides, and sphingomyelin and other sphingolipids. Prosaposin also exists as a secretory protein in body fluids. In this investigation prosaposin was expressed in Spodoptera frugiperda cells (Sf9) by infection with baculovirus containing a full length cDNA coding for human prosaposin. Prosaposin was isolated and purified from spent culture medium of the recombinant Sf9 cell cultures as well as from human seminal plasma and milk. From sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight of both native human prosaposins is estimated to be 66 kDa and that of recombinant prosaposin as 58 kDa. Deglycosylation of native and recombinant prosaposins yielded a protein with a molecular weight of 54 kDa and isoelectric point of 5.4. The N-terminal sequence of both native and recombinant prosaposins was identical (G-P-V-L-L-G-L-K). Like mature saposins, all prosaposins possessed stimulative activity for cerebroside beta-glucosidase (saposins A and C activity), GM1 ganglioside beta-galactosidase (saposin B activity), and sphingomyelinase (saposin D activity) but not sulfatide sulfatase (saposin B activity). Partially proteolyzed products derived from prosaposins were isolated and identified. From seminal plasma, two proteins of 48 and 29 kDa and from Sf9 culture media, two proteins of 39 and 26 kDa were characterized. N-terminal amino acid sequencing and Western blot analysis of each protein indicated that the 39-and 48-kDa proteins are cleavage products containing domains for saposins B, C, and D (trisaposins), and the 26- and 29-kDa proteins are cleavage products containing domains for saposins C and D (disaposin). These observations suggest that proteolysis of prosaposin in these tissues occurs sequentially from the N-terminal region. Proteins involved in the initial proteolysis of prosaposin were partially characterized in human testis.
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PMID:Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins). 832 76


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