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)

In three profiles of a semi-gley soil under the floodplain forest, variations were studied in the activities of invertase, amylase, cellobiase, cellulase, proteases, and phosphatases. In the surface soil layer, enzymatic activity was found affected by the soil moisture at a significant level, whereas in the deeper soil layers the influence of aeration was more effective. Moreover, significant correlations could be detected between the amount of available nitrogen and protease activity, while the water-soluble phosphorus acted as a represeive agent on the activity of phosphatases. Existence of correlations between the numbers of microbes and enzymes could be demonstrated for invertase and protases only.
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PMID:Enzymatic activity in a semi-gley soil under the floodplain forest in South Moravia. 20 42

The in situ lipid activator of rat liver glucocerebrosidase was investigated. Rat liver lysosomes were purified (42.9-fold relative to the crude homogenate) by sequential isopycnic centrifugation in sucrose and metrizamide gradients. Lipids were extracted with chloroform:methanol (2:1) and phospholipids were separated by one-dimensional thin-layer chromatography. The phospholipid content of the lysosome preparation was 0.28 mumol lipid phosphorus/mg protein. Phosphatidylcholine was present as the major nonacidic phospholipid (39.3%). Of the acidic phospholipids, phosphatidylinositol and phosphatidylserine were present in the greatest amounts (12.0 and 19.7%, respectively). The resolved phospholipids were tested separately and in the presence of a heat-stable factor from Gaucher spleen for their ability to reconstitute butanol-delipidated rat liver glucocerebrosidase activity. Alone or in the presence of the heat-stable factor, phosphatidylserine and phosphatidylinositol were the most effective activators of glucocerebrosidase. Bis(monoacylglyceryl) phosphate derived from rat liver tritosomes or rabbit lung macrophages was also effective in reconstituting beta-glucosidase activity.
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PMID:Comparison of the ability of phospholipids from rat liver lysosomes to reconstitute glucocerebrosidase. 395 63

The group O streptococcal group antigen was shown to be a polysaccharide located in the cell wall of the organism. The antigen could be extracted by one of several methods: (i) 0.5 n NaOH at 37 C, (ii) phenol-water (50:50) at 68 C, (iii) 0.2 n HCl at 100 C, or (iv) 10% trichloroacetic acid at 4 C. The last method yielded more polysaccharide with less protein contamination. The polysaccharide was purified on diethylaminoethyl-Sephadex A-25 and Sephadex G-200. It was composed of two-thirds glucosamine and galactosamine, and the remainder glucose plus galactose. Rhamnose, glycerol, ribitol, and muramic acid were absent. Total phosphorus and amino acids were each less than 0.1%. N-Acetyl-beta-d-glucosamine exerted a strong inhibition of the precipitin reaction and is considered the immunodominant sugar. Glucosamine and glucose possessed a partial inhibitory activity. Galactose and galactosamine were essentially negative. No evidence of cross-reactivity was found between the O polysaccharide and group A and L polysaccharides, and group A and Staphylococcus aureus teichoic acids, which posesss N-acetylglucosamine specificity. The release of limited quantities of N-acetyl-glucosamine from its terminal location by enzyme, and glucose by acid hydrolysis, indicates a limited number of side chains in the O antigen. The glucosamine is in acid-stable linkage in the polysaccharide. Glucose was not released by beta-glucosidase and probably does not occupy a terminal position. The O antigen is the only known streptococcal polysaccharide antigen which does not contain rhamnose. The effect of these factors on the immunological specificity is discussed. O serum, after adsorption with the purified polysaccharide, was used to demonstrate the presence of protein antigens in acid extracts of cells from each of the nine strains examined. These antigens may represent type antigens. Two of these strains, originally described as group O, did not contain the O polysaccharide.
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PMID:Chemical composition and immunological specificity of the streptococcal group O cell wall polysaccharide antigen. 462 49

Little is known about the potential of enzyme activities, which are sensitive to soil properties and management, for the characterization of dust properties. Enzyme activities may be among the dust properties key to identifying the soil source of dust. We generated dust (27 and 7 microm) under controlled laboratory conditions from agricultural soils (0-5 cm) with history of continuous cotton (Gossypium hirsutum L.) or cotton rotated with peanut (Arachis hypogaea L.), sorghum [Sorghum bicolor (L.) Moench], rye (Secale cereale L.), or wheat (Triticum aestivum L.) under different water management (irrigated or dryland) and tillage (conservation or conventional) systems. The 27- and 7-microm dust samples showed activities of beta-glucosidase, alkaline phosphatase, and arylsulfatase, which are related to cellulose degradation and phosphorus and sulfur mineralization in soil, respectively. Dust samples generated from a loam and sandy clay loam showed higher enzyme activities compared with dust samples from a fine sandy loam. Enzyme activities of dust samples were significantly correlated to the activities of the soil source with r > 0.74 (P < 0.01). The arylsulfatase proteins contents of the soils (0.04-0.65 mg protein kg(-1) soil) were lower than values reported for soils from other regions, but still dust contained arylsulfatase protein. The three enzyme activities studied, as a group, separated the dust samples due to the crop rotation or tillage practice history of the soil source. The results indicated that the enzyme activities of dust will aid in providing better characterization of dust properties and expanding our understanding of soil and air quality impacts related to wind erosion.
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PMID:Enzyme activities and arylsulfatase protein content of dust and the soil source: biochemical fingerprints? 1535 25

Temporal oscillations in hydrology are a common occurrence in wetlands and can result in alternating flooded and drained conditions in the surface soil. These oscillations in water levels can stimulate microbial activities and result in the mobilization and redistribution of significant amounts of carbon (C), nitrogen (N), and phosphorus (P). The goal of this study was to experimentally simulate a drawdown and reflood of marsh soil from a nutrient-enriched site and a reference site of a wetland (Blue Cypress Marsh Conservation Area, Florida). The goal was to better understand the changes in biogeochemistry and microbial activities present in these soils as a result of hydrological fluctuations. Measurements of dissolved reactive phosphorus (DRP), ammonia, and nitrate in the floodwater indicated significantly higher (alpha = 0.05) NH(4)(+) and DRP fluxes from the nutrient-enriched site; floodwaters in the cores from both sites contained significant NO(3)(-) concentrations (9.6 mg N L(-1)), which was rapidly consumed over the core incubation period (30 d). Water level drawdown and reflooding initially stimulated the soil microbial biomass, methanogenic rates, and extracellular enzyme activities (acid phosphatase and beta-glucosidase). The anaerobic microbial metabolic activities (CO(2)) where initially significantly (alpha = 0.05) enhanced by the reflood, resulting in roughly equivalent rates as the aerobic respiratory activities (CO(2)), presumably as a function of the high water column NO(3)(-) levels. This study illustrates that the reflood event in the hydrological cycles in a wetland can significantly stimulate the activities of hydrolytic enzymes and microbiological communities in these soils.
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PMID:Response of biogeochemical indicators to a drawdown and subsequent reflood. 1553 59

A field experiment was carried out to assess the effectiveness of the addition of sugar beet, rock phosphate, and Aspergillus niger directly into the planting hole, and the mycorrhizal inoculation of seedlings with Scleroderma verrucosum, for promotion of plant growth of Cistus albidus L. and Quercus coccifera L. and enhancement of soil physicochemical, biochemical, and biological properties, in a degraded semiarid Mediterranean area. One year after planting, the available phosphorus content in the amended soils of both species was about fourfold higher than in the nonamended soil. Amendment addition increased the aggregate stability of the rhizosphere of C. albidus (by 56% with respect to control soil) while the mycorrhizal inoculation increased only the aggregate stability of the rhizosphere of Q. coccifera (by 13% with respect to control soil). Biomass C content and enzyme activities (dehydrogenase, urease, protease-BAA, acid phosphatase, and beta-glucosidase) of the rhizosphere of C. albidus were increased by amendment addition but not by mycorrhizal inoculation. Both treatments increased enzyme activities of the rhizosphere of Q. coccifera. The mycorrhizal inoculation of the seedlings with S. verrucosum was the most effective treatment for stimulating the growth of C. albidus (by 469% with respect to control plants) and Q. coccifera (by 74% with respect to control plants). The combined treatment, involving mycorrhizal inoculation of seedlings and addition of the amendment directly into soil, had no additive effect on the growth of either shrub species.
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PMID:Establishment of two ectomycorrhizal shrub species in a semiarid site after in situ amendment with sugar beet, rock phosphate, and Aspergillus niger. 1569 Feb 28

We tested whether seasonal changes in the sources of organic substances for microbial metabolism were reflected changes in the activities of five extracellular enzymes in the eighth order lowland River Elbe, Germany. Leucine aminopeptidase showed the highest activities in the water column and the sediments, followed by phosphatase > beta-glucosidase > alpha-glucosidase > exo-1,4-beta-glucanase. Individual enzymes exhibited characteristic seasonal dynamics, as indicated by their relative contribution to cumulative enzyme activity. Leucine aminopeptidase was significantly more active in spring and summer. In contrast, the carbohydrate-degrading enzymes peaked in autumn, and beta-glucosidase activity peaked once again in winter. Thus, in sediments, the ratio of leucine aminopeptidase/beta-glucosidase reached significant higher medians in spring and summer (5-cm depth: ratio 7.7; 20-cm depth: ratio 10.1) than in autumn and winter (5-cm depth: ratio 3.7, 20-cm depth: ratio 6.3). The relative activity of phosphatase in the sediments was seasonally related to both the biomass of planktonic algae as well as to the high content of total particulate phosphorus in autumn and winter. Due to temporal shifts in organic matter supply and changes in the storage capacity of sediments, the seasonal peaks of enzyme activities in sediments exhibited a time lag of 2-3 months compared to that in the water column, along with a significant extension of peak width. Hence, our data show that the seasonal pattern of extracellular enzyme activities provides a sensitive approach to infer seasonal or temporary availability of organic matter in rivers from autochthonous and allochthonous sources. From the dynamics of individual enzyme activities, a consistent synoptic pattern of heterotrophic functioning in the studied river ecosystem could be derived. Our data support the revised riverine productivity model predicting that the metabolism of organic matter in high-order rivers is mainly fuelled by autochthonous production occurring in these reaches and riparian inputs.
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PMID:Regulation and seasonal dynamics of extracellular enzyme activities in the sediments of a large lowland river. 1620 47

We tested the hypothesis that the appearance of mucilage in the Northern Adriatic Sea was related with the accumulation of dissolved organic compounds released by intensive enzymatic activities and not utilized as direct substrate for microbial growth. To do this enzymatic activities and dissolved organic and inorganic pools in periods characterized by the presence of mucilage and in the same seasons but in absence of mucilage were compared. Extracellular enzymatic activities (aminopeptidase, beta-glucosidase and alkaline phosphatase), nutrient pool concentrations (total dissolved nitrogen, dissolved organic nitrogen, total dissolved phosphorus, dissolved organic phosphorus) and the biochemical composition of particulate and dissolved organic matter (in terms of proteins and carbohydrates) were determined on a monthly basis over a period of 3 years. Aminopeptidase and alkaline phosphatase activities displayed higher values in springs preceding the appearance of mucilage than in spring when no mucilage was observed. Beta-Glucosidase activity showed significantly higher values in summer periods characterized by the massive production of mucilage than in summers without mucilage events. The months preceding mucilage events were also characterized by an increase of the alkaline phosphatase to aminopeptidase activity ratio and by a significant accumulation of dissolved proteins. These findings, together with the significant increase of the DON/DOP ratio, suggest that mucilage formation is favoured by the deficiency of organic P. The present study provides compelling evidences that mucilage formation is favoured by the unbalance between organic matter mobilization by enzymatic activities and the accumulation of labile dissolved organic-N compounds.
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PMID:Exo-enzymatic activities and dissolved organic pools in relation with mucilage development in the Northern Adriatic Sea. 1622 8

The streptococcal group E cell wall polysaccharide antigen was extracted from strain K129 cells with hot trichloroacetic acid and purified. It contained rhamnose and glucose in a 2:1 molar ratio, 2% protein, 1% phosphorus, and was free of muramic acid and glycerol. No type polysaccharide antigen was present. The reaction of specific group E rabbit antiserum with the polysaccharide was effectively inhibited by d-glucose and beta-glucosides such as 1-methyl-beta-d-glucose, cellobiose, and gentiobiose. The 1-methyl-alpha-d-glucose was one-half as effective as the beta isomer. l-Rhamnose and N-acetyl-d-glucosamine were ineffective. Partial acid hydrolysis of the antigen followed by chromatographic separation of the oligosaccharides resulted in the isolation and analysis of five fractions. These fractions were di-, tri-, and tetrasaccharides. A study of these fractions by chemical analysis, reduction with borohydride, inhibition of the antigen-antibody reaction, release of glucose by beta-glucosidase, and other evidence indicate that beta-d-glucose is the immunodominant sugar in the antigen. A glucose-rhamnose trisaccharide (1:2 molar ratio) was the most effective inhibitor of the precipitin reaction; the glucose was readily released by beta-glucosidase, and one-half of the rhamnose was reduced with borohydride. This trisaccharide is considered to be a repeating unit in the native polysaccharide and probably has the following structure: O-beta-d-glucosyl-(1-2)-O-alpha-l-rhamnosyl- (1-4)-l-rhamnose. A glucose-rhamnose disaccharide in which the hexose and pentose are linked as in the trisaccharide was an effective inhibitor of the precipitin reaction. Strain K129 cells do not appear to contain a type polysaccharide antigen.
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PMID:Chemical structure and immunological specificity of the streptococcal group e cell wall polysaccharide antigen. 1655 32

Protein bodies and spherosomes isolated from mature seeds of Sorghum bicolor (Linn.) Moench have measurable activity of acid protease, alpha-glucosidase, beta-glucosidase, beta-galactosidase, phytase, acid pyrophosphatase, p-nitrophenyl phosphatase, and RNase. Protein bodies have largely insoluble activities, and produce soluble protein and soluble amino nitrogen during autolysis. They have the dual function of protein storage and protein catabolism. Spherosomes have considerable amounts of soluble enzymes and autolytically produce soluble amino nitrogen and inorganic phosphate but release little soluble protein. Spherosomes are similar to animal lysosomes but have an additional storage function for protein, phosphorus, and metals. Mature sorghum seed contains the necessary enzymes and substrates to generate two basic metabolites, amino acids and inorganic phosphate.
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PMID:Acid Hydrolases and Autolytic Properties of Protein Bodies and Spherosomes Isolated from Ungerminated Seeds of Sorghum bicolor (Linn.) Moench. 1665 31


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