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)

Optimal assay conditions are described for 8 hydrolases of Euglena gracilis var. bacillaris, SM-L1 (streptomycin-bleached) strain, 7 of which have an acid pH-optimum. Acid-phosphatase, beta-galactosidase, beta-glucosidase, b-fucosidase, cathepsin D, RNase, DNase, and an esterase are active in cell homogenates. Amylase has very low activity, and beta-glucuronidase, arylsulfatase, beta, N-acetyl-glucosaminidase, alpha-fucosidase, and alpha- and beta-mannosidase are inactive.
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PMID:Hydrolytic enzymes of Euglena gracilis: characterization and activity as a function of culture age and carbon deprivation. 0 4

The exudates or liquid droplets on various structures of a number of fungi were examined. The droplets were enveloped in membranous material and were associated with actively growing mycelia, including fruiting structures. Osmium tetroxide vapour-fixed droplets of Claviceps purpurea, Myrothecium roridum, Sclerotinia sclerotiorum, Sclerotium rolfsii, and Thanathephorus cucumeris did not dry to a powder but remained intact as spheres when freeze-dried. Fractured spheres, examined with the scanning electron microscope, showed the presence of a membranous structure similar to that of rapidly frozen colloidal solutions with the ice crystals removed by sublimation. Locules or cavities within the freeze-dried droplets are thought to be due to the entrapment of air when droplets coalesce. Biochemical analyses of the exudates showed that acid phosphatase, beta-glucosidase, acid and alkaline protease. RNase polygalacturonase and cellulase enzymes as well as oxalic acid and ammonia were present.
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PMID:Fungal exudates. 72 49

Homogenates of Giardia lamblia trophozoites exhibited the following hydrolase activities: acid phosphatase (EC 3.1.3.2), proteinase (EC 3.1.4) with urea-denatured hemoglobin and N-benzoyl-DL-arginine-2-naphthylamide as substrates, deoxyribonuclease (EC 3.1.4.5), and ribonuclease (EC 2.7.7.16). beta-N-Acetylglucosaminidase (EC 3.2.1.30), beta-galactosidase (EC 3.2.1.23), beta-glucuronidase (EC 3.2.1.31), alpha-D-glucosidase (EC 3.2.1.20), beta-D-glucosidase (EC 3.2.1.21), and beta-D-xylosidase (EC 3.2.1.37) activities were below the level of detection. Differential and isopycnic centrifugation of homogenates demonstrated that giardial hydrolases were localized in a single-particle population sedimenting at 7200g for 30 min. The particles had a buoyant density in sucrose of 1.15 and exhibited latency. Latency was completely destroyed by Triton X-100 or 15 cycles of freezing and thawing. After centrifugation of Triton- or freeze-thaw-treated particle fractions, the hydrolase activities, though no longer latent, were still sedimentable suggesting tight binding to the organelle membrane. Latency was destroyed simultaneously for all hydrolases, in direct proportion to the amount of Triton added to a particle preparation or to the number of times a particle preparation was subjected to freezing and thawing. These results support the suggestion that the hydrolases of G. lamblia trophozoites are localized in a single-particle population of lysosome-like organelles.
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PMID:Giardia lamblia: localization of hydrolase activities in lysosome-like organelles of trophozoites. 327 50

Axenic Tetrahymena pyriformis, syngen 1, mating type II cells were grown in Cox's defined medium. When washed and transferred into nonnutrient dilute salt solution or resuspended in the defined medium, the intact cells secrete acid hydrolases into the medium. Cells starving in the salt solution release in 5 hr about two-thirds of their beta-glucosidase, beta-N-acetylglucosaminidase, alpha-glucosidase, and amylase activities, about one-third of their deoxyribonuclease and phosphatase activities, smaller amounts of ribonuclease, and only a negligible fraction of their proteinase activity and protein content. During this period there is practically no change in the enzyme activities (except for a sudden increase of ribonuclease activity) and protein content of cells and medium together. Cells resuspended in the nutrient medium secrete enzymes as do the starved cells, but replace this loss, so that there is a continuous increase of the activities in the total system. According to isopycnic centrifugation experiments performed in sucrose gradients, the source of the hydrolases is a special population of lysosomes which disappear from the cells during starvation. This population equilibrates in the high density region of the gradients and contains the various acid hydrolases in about the proportion in which these enzymes appear in the medium.
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PMID:Secretion of acid hydrolases and its intracellular source in Tetrahymena pyriformis. 433 53

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

An enzymatic profile of 20 strains of Pseudomonas maltophilia was undertaken with conventional plate tests, API ZYM, and 4-methylumbelliferyl-conjugated substrates. All strains produced DNase, RNase, arbutinase, esterases and lipases, mucinase, acid and alkaline phosphatases, alkaline pyrophosphate diesterase, phosphoamidase, beta-glucosidase, leucine arylamidase, and acetatase and were hemolytic for horse, sheep, and rabbit blood. The majority of strains produced chitinase, hyaluronidase, albuminase, valine arylamidase, trypsin, alpha- and beta-glucosidases, and N-acetyl-beta-glucosaminidase. API ZYM and 4-methylumbelliferyl-conjugated substrate assays are rapid, simple, specific, and sensitive and may be useful as diagnostic aids in the identification of P. maltophilia and other pseudomonads.
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PMID:Enzymatic profile of Pseudomonas maltophilia. 681 50

By using a suckling mouse assay, heat-stable enterotoxin (ST) was purified from the culture filtrate of Yersinia enterocolitica isolated from a diarrheal patient. The purification procedures involve ultrafiltration with an Amicon HIP-10 hollow fiber, ethanol fractionation, protamine sulfate treatment, diethylaminoethyl-Sephacel and hydroxylapatite column chromatographies, and Sephacryl S-200 superfine gel filtration. About 408-fold purification was achieved, with a yield of 12.0%. The minimal effective dose of purified ST was about 110 ng in the suckling mouse assay. The molecular weight of purified ST was 9,000 by Sephadex G-100 superfine gel filtration. The purified ST was stable to heating (100 degrees C for 20 min, 121 degrees C for 20 min) and did not lose its toxicity after treatment with protease, trypsin, lipase, phospholipase C, ribonuclease, deoxyribonuclease, beta-glucosidase, and neuraminidase. The purified ST was separated by isoelectric focusing into two active fractions, with pI's of 3.29 (ST-1) and 3.00 (ST-2), respectively. Antiserum from guinea pigs immunized with the purified ST neutralized the activity of both Y. enterocolitica ST and Escherichia coli ST.
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PMID:Partial purification and characterization of heat-stable enterotoxin produced by Yersinia enterocolitica. 721 60

We studied the mechanism of growth-stimulating effect of various compounds using an exogenous RNase-micromycete model and found that the treatment with microdoses of RNase intensified the reproduction of the yeast Candida valida and growth of Aspergillus fumigatus. At the same time the respiration activity of yeast cells and fungal mitochondria as well as succinate dehydrogenase activity increased. The secretion of total protein, cellulase and cellobiase changed in the presence of RNase in the growth medium. Electrophoretic mobility of Candida valida cells enhanced by 20%. The RNase stimulating effect on microbial cells seems to result from changes in characteristics of the cell surface.
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PMID:[The action of exogenous RNAse on the cells of lower eukaryotes]. 848 61

Membranes were prepared from tissues of the carp Ctenopharynogodon idellus including liver, kidney, intestine, adipose tissue, ovary, gill, heart, muscle and spleen. The carp liver and intestine membranes bound 125I-labeled bovine growth hormone and the binding could be displaced by cold bovine growth hormone. No changes in the ability to bind 125I-labeled bovine growth hormone occurred after treatment of the carp liver membrane with DNase, RNase, alpha-amylase and beta-glucosidase, suggesting that neither nucleic acids nor carbohydrates played an important part in the hepatic binding of growth hormone. Treatment of carp liver membranes with either chymotrypsin or trypsin produced a decrease in the growth hormone binding activity, indicating that the growth hormone receptor on carp liver membrane is a protein. Treatment of carp liver membranes with p-chloromercuribenzoate brought about a reduction in 125I-bGH binding. The inhibition could be reversed by dithioerythritol, suggesting the involvement of essential sulfhydryl group in bGH binding.
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PMID:Presence of growth hormone receptors in carp liver and intestine. 849 May 77

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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