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)

Some properties of a number of enzymes immobilized by the diazotized m-diaminobenzene (dDAB) method are described. The pH-activity profiles of beta-D-glucosidase, glucoamylase, peroxidase, uricase, and D-glucose oxidase were virtually unchanged on immobilization while those of catalase and dextranase were significantly altered. beta-D-Glucosidase, glucoamylase, and glucose oxidase were found to be more susceptible to denaturation on lyophilization when immobilized than in the native state; however, sorbitol had a marked protective effect in every case examined. Sorbitol was also found to exert a stabilizing effect when lyophilized immobilized preparations were stored. Immobilization marginally improved the stabilities of a number of enzymes to heating at 60 degrees at pH 8.0. The usefulness for continuous reaction of a column of glucoamylase attached to celite was established. The reuse of the solid supports was demonstrated.
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PMID:Properties of enzymes immobilized by the diazotized m-diaminobenzene method. 1 49

Isolates of Cephalosporium maydis varied in their pathogenicity to D.C. 67 maize cultivar from highly to weakly pathogenic. Highly pathogenic isolates showed lower activity of polyphenol oxidase, peroxidase, cytochrome oxidase, and beta-glucosidase enzymes and higher activity of catalase and dehydrogenase than weakly pathogenic isolates. Enzymes production by the tested isolates increased as the culture age increased; except in case of catalase enzyme, the reverse action was detected. The role of these enzymes in the virulence of C. maydis is suggested and discussed.
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PMID:The role of certain oxidative enzymes, catalase, and beta-glucosidase on virulence of Cephalosporium maydis. 9 10

Eschscholtzia californica stigmas with germinating pollen at different stages of development were the subject of histochemical studies which aimed the localization of several enzymes like phosphorylase, leucine amino peptidase, nonspecific esterase, cytochrome oxidase, aldolase, alpha-glycerophosphate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, monoamine oxidase, alpha-galactosidase, beta-glucosidase and beta-galactosidase. Pollen and pollen tubes were shown to contain starch, lipid, proteins and soluble sugars as the storage products. These storage products were utilized during germination and tube growth. The role of different enzymes in the process of germination and tube growth is discussed. From the distribution of oxidoreductases it is inferred that respiration plays an essential role in the tube growth. During pollen germination probably the reserve proteins were transported to pollen tube tip. The increase of activity of alpha-and beta-galactosidase in pollen tubes indicates on their involvement in carbohydrate metabolism. The role of alpha-galactosidase in the metabolism of galactolipids is also inferred. Similarly, the reaction catalysed by beta-glucosidase resulted in the production of aglycon and glucose; of these the former possibly act as a substrate of peroxidase. Some of the glycosidases diffused out of pollen wall on the stigma and participated in the release of free sugars of the female tissue.
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PMID:Studies on the physiology of pollen and pollen tube growth. IV Eschscholtzia californica Cham. 22 Jan 58

Two filamentous fungi, the white-rot fungus Trametes versicolor and the soil fungus and potential biocontrol organism Trichoderma harzianum, have been grown in pure and mixed cultures on low-N (0.4 mM) and high-N (4 mM) defined synthetic media to determine the activities of selected wood-degrading enzymes such as cellobiase, cellulase, laccase, and peroxidases. Growth characteristics and enzyme activities were examined for potential correlations. Such correlations would allow the use of simple enzyme assays for measuring biomass development and would facilitate predictions about competitiveness of species in mixed fungal cultures. Our results show that while laccase and Poly Red-478 peroxidase activities indicate survival of the decay fungus, none of the monitored extracellular enzymes can serve as a quantitative indicator for biomass accumulation. As expected, the level of available nitrogen affected the production of the enzymes monitored: in low-N media, specific cellobiase, specific cellulase, and peroxidase activities were enhanced, while laccase activities were reduced. Most importantly, laccase activities of Trametes versicolor, and to a smaller extent, cellobiase activities of both fungi, were significantly induced in mixed cultures of Trametes versicolor and Trichoderma harzianum.
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PMID:Changes in selected enzyme activities during growth of pure and mixed cultures of the white-rot decay fungus Trametes versicolor and the potential biocontrol fungus Trichoderma harzianum. 161 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

Methods for the characterization of catalase, peroxidase, beta-glucosidase, esterase, and beta-lactamase mycobacterial isoenzymes were described. These methods were applied to examine strains of the M. fortuitum complex. M. fortuitum, M. peregrinum, M. chelonae- M. abscessus and an unnamed species had distinct isoenzyme profiles. M. chelonae and M. abscessus could not be satisfactorily differentiated using the described methods.
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PMID:Isoenzymes as tools to discriminate various subdivisions in the Mycobacterium fortuitum complex. 254 63

A procedure for the immunoassay of cohydrolase sphingolipid-I in mouse tissue is described. This cohydrolase (actually a mixture of at least four related proteins) stimulates or activates the beta-glucosidase which hydrolyzes ceramide glucoside, a widely occurring glycosphingolipid. The method involves extraction of cohydrolase from tissue homogenate with a salt-buffer solution, removal of proteins by adjustment to pH 6, further removal of proteins by heating, and removal of interfering materials with a small size exclusion column. Antibodies were raised to bovine cohydrolase in rabbits and purified with an affinity column made from cohydrolase. The immunoassay involves binding of antibody by the cohydrolase sample (20-200 pg) in competition with cohydrolase that has been chemically linked to horseradish peroxidase. The mixture is treated with particle-linked second antibody and centrifuged; the pellet is then assayed fluorometrically for peroxidase content. Initial application of the method showed that cohydrolase was present in all mouse tissues studied and that its concentration paralleled that of glucocerebrosidase relatively closely. Changes with age (14 and 92 days) occurred in a similar fashion for the two substances.
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PMID:Determination of the glucosidase-stimulating proteins by competitive enzyme-linked immunoassay. 639 20

A simple and rapid method for determining the cellobiase activity in purified enzyme preparations was developed. It is based on a series of consecutive enzymatic reactions, i. e. hydrolysis of cellobiose by cellobiase, oxidation of the forming glucose by glucose oxidase, and formation of a dyed product under peroxidase action in the same reaction system. The dyed product is recorded spectrophotometrically at 460 nm. One measurement takes from 2-3 to 7-10 min depending on a particular method of the activity determining. The reagent which is used for the activity determining can be obtained in the yophylized form and used repeatedly. The relative deviation of the method is 5-7%.
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PMID:[Rapid method for determining cellobiase activity]. 642 19

A pancreas-specific antigen was identified by immunologic techniques and purified from saline extract of human pancreas. The purified pancreas-specific antigen was shown to be homogeneous by polyacrylamide gel electrophoresis under both denaturing and non-denaturing conditions. It had a molecular weight of 44000 as estimated by gel filtration or sodium dodecyl sulfate-gel electrophoresis, and a sedimentation coefficient of 3.4 S as analyzed by sucrose gradient centrifugation. Pancreas-specific antigen possessed an isoelectric point of 4.9 and migrated to alpha-beta region upon immunoelectrophoresis. By colorimetric assay procedures, pancreas-specific antigen exhibited no enzyme activity, such as amylase, protease, esterase, lipase, acid phosphatase, alkaline phosphatase peroxidase, deoxyribonuclease or ribonuclease. Immunoreactivity of pancreas-specific antigen was sensitive to proteolytic enzymes, perchloric acid and high temperature (70 degrees C, 10 min); but insensitive to neuraminidase or beta-glucosidase. Immunohistochemical staining revealed that pancreas-specific antigen was located in acinar cells of human pancreas. In addition, a higher concentration of pancreas-specific antigen was detected in pancreatic juice than in the saline extract of pancreas. This newly identified pancreas-specific antigen, therefore, may be a useful marker protein in physiological studies of pancreas and pancreatic secretion.
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PMID:Purification and characterization of a human pancreas-specific antigen. 678 69

A pancreas cancer-associated antigen (PCAA) was identified and isolated from ascites fluid of human pancreatic cancer. Purified PCAA was homogeneous as determined by polyacrylamide gel electrophoresis. PCAA was a glycoprotein with a molecular weight of approximately 1,000,000 and consisted of 20% carbohydrates and 80% peptides, had an isoelectric point of 4.7, and migrated to alpha 2-beta region. It possessed a sedimentation coefficient of 14S and appeared to be a fibrous or fibroglobular protein. Immunoreactivity of PCAA was sensitive to proteolytic enzymes, perchloric acid, KSCN, glycine-HCl at pH 2.5, urea and lithium diiodosalicylate; and insensitive to neuraminidase or beta-glucosidase. Immunohistochemical technique revealed that PCAA was located in the cytoplasm of ductal epithelial cells of malignant pancreas. Using heteroantiserum raised against purified PCAA, horseradish peroxidase and CNBr-activated Sepharose 4B, an enzyme-immunoassay (EIA) for circulating PCAA has been developed. From a group of 40 healthy blood donors, an upper limit of 16.2 micrograms of PCAA/ml of serum has been tentatively determined. An elevated PCAA was shown in 67% (29/43) of patients with pancreas cancer, as well as in 30% (11/36) of lung cancer patients, 27% (10/37) of colonic cancer patients, and in 16% (6/36) of breast cancer patients. The reactive antigen in sera of these cancers was shown to be immunologically identical. PCAA also was detected in extracts of various human tissues, particularly pancreatic tumors, colonic tumors, and in a normal colon. Further, PCAA exhibited heterogeneity in molecular weight, isoelectric point, and electrophoretic mobility.
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PMID:Isolation, characterization and clinical evaluation of a pancreas cancer-associated antigen. 702 47


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