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 enzymatic activity of acid cathepsins, hyaluronidase, beta-D-glucuronidase, alpha-D- and beta-D-glucosidases in blood serum as well as some of these activities in the synovial fluid, liver tissue and spleen were determined in different periods of adjuvant arthritis, in rats. In the first days of arthritis (the acute stage) in rats the activity of hyaluronidase, beta-D-glucuronidase, and acid cathepsins in blood serum, that of hyaluronidase and acid cathepsins in the synovial fluid as well as of acid cathepsins in the spleen tissues were increased. The found inhibition of the beta-D-glucosidase activity in blood serum, synovial fluid and spleen tissue, alpha-D-glucosidase activity in the liver tissue against a background of activation of acid cathepsins, hyaluronidase, beta-D-glucuronidase in blood serum, of acid cathepsins, hyaluronidase, beta-D-glucuronidase in the synovial fluid as well as acid cathepsins in the spleen is associated with the further development of the pathological process and characterizes the adjuvant arthritis chronic stage. The alpha-D-glucosidase activity in blood serum is exception, its inhibition is manifested from the third day of arthritis.
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PMID:[Activity of acid hydrolases in rat tissues under experimental arthritis]. 678 24

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

The authors performed a comparative biochemical study of some enzymes of lysosomic origin (hyaluronidase, N-acetyl-beta-D-glucosaminidase, beta-glucosidase, beta-galatosidase and acid phosphatase), of the state of enzyme substrate system N-acetylneuraminic acid---aldolase of neuramic acid and of the activity of lactatedehydrogenase (soluble in cytosol and bound on mitochodria) in the liver, lungs and blood serum of rats at various regimens of the inhalation action of CCl4. On the basis of results obtained they determined the biological importance of the change of activity of enzymes differently localized in cells at the adaptation of an organisme to the noxious action of CCl4.
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PMID:The influence of tetrachloromethane on subcellular structures of rat hepatocyte lysosomal and cytoplasmic enzymes of the liver, lungs and blood serum of rats during continuous and intermittent action of tetrachloromethane. 719 Sep 85

Members of the Streptococcus sanguis group (SSG) and Streptococcus milleri group (SMG) were screened for their ability to produce glycosidase, arylamidase (peptidase), protease, dextranase and glycosyltransferase activities. Species within each group produced unique patterns of activity. The most commonly produced glycosidases were beta-D-glucosidase, beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase and the least commonly produced glycosidase activity was beta-fucosidase with Streptococcus intermedius (SMG) being the only species capable of producing the activity. For arylamidase activity, the most commonly produced type was lysine-arylamidase. Glycosidase and arylamidase activities were localized to particular sub-cellular fractions. alpha-galactosidase was found only in culture supernatant fluids whereas N-acetyl-beta-D-glucosaminidase was found in all fractions; the culture supernatant, cell wall, cell membrane and cytoplasm. No arylamidase activity was seen in culture supernatants. Phe-arg-arylamidase was found only in cytoplasmic fractions whereas val-pro-argarylamidase was found in cell walls, cell membranes and cytoplasmic fraction. Protease activity was measured as the degradation of bovine serum albumin (BSA) and casein. Casein was degraded by a number of strains whereas no species/strains were able to degrade BSA. Streptococcus intermedius, Streptococcus constellatus (SMG), Streptococcus mitior and Streptococcus defectivus (SSG) were the only species that produced hyaluronidase and no species produced chondroitin sulphatase. The groups were also examined for their abilities to produce glycosyltransferase and dextranase. Strep. sanguis, Streptococcus gordonii, Streptococcus mitis and Streptococcus oralis produced glucosyltransferase and, with the exception of the latter species, fructosyltransferase. No species within the SMG was capable of producing either glycosyltransferase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Degradative enzymes of oral streptococci. 778 31

1. In human plasma, an enzyme is present which hydrolyzes 4-methylumbelliferyl-tetra-N-acetylchitotetraoside. The function of this enzyme is unknown. 2. We have examined whether hyaluronidase, neutral endoglucosaminidase, N-acetyl-beta-D-hexosaminidase, aspartylglucosaminidase, beta-D-glucosidase, and chitobiase could hydrolyze MU-TACT. The results obtained are detailed below. 3. A purified commercial preparation of hyaluronidase does not hydrolyze MU-TACT. 4. Substrate specificity requirements, pH optimum and subcellular localization indicate that neutral endoglucosaminidase is distinguishable from MU-TACT hydrolase. Also commercial neutral endoglucosaminidase D and H have no affinity towards MU-TACT. 5. N-Acetyl-beta-D-hexosaminidase is different from MU-TACT hydrolase for the following reasons: (a) a purified enzyme preparation does not hydrolyze MU-TACT; (b) there is no correlation in the activity of the enzymes; (c) MU-TACT hydrolase is not deficient in cells of a patient with a deficiency of total N-acetyl-beta-D-glucosaminidase; and (d) the 2 enzymes have very different chromatographic characteristics and Con A binding properties. 6. Enzyme characteristics, substrate structural requirements and a lack of correlation with MU-TACT hydrolase activity suggest that aspartylglucosaminidase, beta-D-glucosidase, and chitobiase are not involved in the hydrolysis of MU-TACT. 7. None of the enzymes which we have considered corresponds to MU-TACT hydrolase. The exact nature and the function of the enzyme remains an enigma.
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PMID:Evaluation on the hydrolysis of methylumbelliferyl-tetra-N-acetylchitotetraoside by various glucosidases. A comparative study. 843 79

Ten Basidiobolus ranarum (= Basidiobolus haptosporus) strains, isolated from faeces of 102 different lower vertebrates (ectotherms) exhibited in Antwerp Zoo, or from their environment were studied for their temperature requirements, haemolysis and other enzyme activities in vitro. All isolates grew well at 25 and 37 degrees C. Three strains that produced undulated zygospore walls were haemolytic and positive for hyaluronidase. All the isolates produced urease, N-acetyl-beta-glucosaminidase, trypsin, lipase, lecithinase, gelatinase, collagenase and elastase, but failed to produce amylase, keratinase and beta-glucosidase. Three isolates failed to produce phosphatase. Only one strain failed to produce DNase. Aesculin was not hydrolysed. Chitinase activity was inconclusive. The results of this study illustrate the importance of exotic animals kept in temperate regions as carriers of potentially pathogenic organisms. In addition to the morphological characteristics, the identification can be based on enzymatic profiles. Enzymatic activity detection may help to explain the pathogenic mechanism of the fungus.
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PMID:Isolation of Basidiobolus ranarum from ectotherms in Antwerp zoo with special reference to characterization of the isolated strains. 1042 99

In observations of the movements of the infective third-stage larvae of a rodent parasitic nematode, Strongyloides ratti, on a sodium chloride gradient set up on agarose plates, two types of chemokinetic behavior were seen: a unidirectional avoidance movement on initial placement of the larvae in unfavorable environmental conditions and a random dispersal movement on their placement within an area of favorable conditions. Track patterns were straight in the avoidance movement but included multiple changes of direction and loops in the dispersal movement. In the present study we examined the interventional activity of treatment with various enzymes, lectins, and chemicals by analyzing the unidirectional avoidance movements of the larvae. We observed that beta-glucosidase, hyaluronidase, beta-galactosidase, trypsin, protease, lipase, phospholipase C, soybean agglutinin, wheat germ agglutinin, and spermidine exerted inhibitory actions on those movements, which may be guided by the chemosensory function of this nematode.
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PMID:Effects of various treatments on the chemokinetic behavior of third-stage larvae of Strongyloides ratti on a sodium chloride gradient. 1109 92

Enzyme inhibitory activities of 14 iridoids previously obtained from two Malaysian medicinal plants, Saprosma scortechinii and Rothmannia macrophylla, were evaluated in vitro using soybean lipoxygenase and bovine testis hyaluronidase. Most of the iridoids, including asperulosidic acid, paederosidic acid, and an epimeric mixture of gardenogenins A and B, did not show any effect on the enzyme activities, except for the bis-iridoids, which inhibited the lipoxygenase activity with their IC(50) values of approximately 1.3 times that of a known inhibitor, fisetin. Structural modification of asperulosidic acid and paederosidic acid through enzymatic hydrolysis by beta-glucosidase resulted in their inhibition towards the enzyme activities, and these activities were enhanced by the presence of some amino acids (lysine, leucine or glutamic acid) or ammonium acetate. Mixtures of gardenogenins A and B; isomers of non-glucosidic iridoids, incubated with amino acid or ammonium acetate did not show any inhibitory effect on the enzyme activities during the 6 h incubation period, except for lysine where spontaneous reaction between the iridoids and amino acid resulted in the inhibition of lipoxygenase activity. The results from these biomimetic reactions suggested that the iridoid aglycons and the intermediates formed by these reactive species could inhibit the enzyme activities, and thus substantiate previous reports that the formation of iridoidal aglycons is a prerequisite for the iridoid glycosides to demonstrate some of the biological activities. In addition, the results also indicated that it is worthwhile to further explore these intermediates as potential anti-inflammatory agents.
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PMID:Effects of iridoids on lipoxygenase and hyaluronidase activities and their activation by beta-glucosidase in the presence of amino acids. 1261 46

The infective third-stage larvae (L3s) of Strongyloides ratti, a parasitic nematode in rodents, showed two types of chemokinesis on a gradient of sodium chloride (NaCl) in an in vitro agarose tracking assay. The types were a consistent directional avoidance behavior under unfavorable environmental conditions and a reduced avoidance behavior under favorable conditions. We examined the effects of treatments with glycolytic enzymes and lectins by analyzing the avoidance behavior. L-Fucose dehydrogenase, hyaluronidase, beta-glucosidase, alpha-mannosidase, beta-galactosidase, concanavalin A, wheat germ agglutinin and soybean agglutinin exhibited inhibitory or enhancive effects on chemokinesis. We also confirmed the sites of the amphids of L3s aside from the mouth at the anterior end by scanning electron microscopy, and that concanavalin A-binding sites existed in the vicinity of the amphids using lectin-histochemistry. The carbohydrate moieties in the amphids of S. ratti L3s may play an important role as chemosensors in perceiving environmental cues.
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PMID:Strongyloides ratti: chemokinesis of glycolytic enzyme- and lectin-treated third-stage infective larvae in vitro. 1586 77

This paper deals with the study of infrasound phonophoresis-induced changes in biochemical factors, which affect the permeability of eyeball tissues. During 10 days, the rabbit right eye was exposed to an infrasound in the changing pressure mode at 4 Hz and 173 dB for 10 minutes every day. The left eye remained control. After finishing a series of studies, the animals were slaughtered, the eyes were enucleated and prepared into individual tissues. Changes in sodium-potassium composition were investigated in the first series. By causing a reduction in the cellular content of K+, infrasound exposure was found to cause a decrease in membranous potential and activation Na-channel, as confirmed by the elevated intracellular levels of Na+. This in turn enhances ocular tissue permeability for drugs without damaging the structure of a cell membrane. Changes in the activity of the following enzymes: beta-glucosidase, cathepsin D, and hy- aluronidase. Infrasound was ascertained to enhance the activity of beta-glucosidase, which accounts for the lower levels of glucose in ocular tissues and points to the activation and acceleration of biochemical processes in the tissues. At the same time the increased concentrations of cathepsin D and hyaluronidase found in ocular tissues were responsible for a temporary reduction in the viscosity of hyaluronic acid, which promotes resolution of opacities, adhesions or scars and increased tissue permeability.
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PMID:[Study of changes in the enzyme-salt composition affecting the permeability of ocular tissues under infrasound phonophoresis]. 1607 26


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