Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

There are two distinct components of the system which limits the rate at which intact cells of S. cerevisiae C hydrolyze external beta-glucosides; one component requires metabolic energy and the other is stereospecific for beta-glucosides. The stereospecific component is localized at the cell membrane, as shown by its sensitivity to heavy metal inhibitors which did not penetrate the cell under the conditions used. It was shown that cellobiose-grown cells were able to remove cellobiose from the medium in which they were incubated, and that the cellobiose uptake system was identical to that which limits the patent beta-glucosidase activity. In order to test the hypothesis that the system in question was a transport system, for beta-glucosides the ability of cellobiose-grown cells to take up (14)C-labeled methyl-beta-glucoside (MBG) was studied. The induced cells were able to take up MBG-(14)C and the label could be partially chased out by cold MBG and cellobiose; glucose-grown cells could not incorporate label. However, induced cells could not take up label when incubated with (14)C-MBG, thus excluding the hypothesis of transport of intact beta-glucosides. It was concluded that the stereospecific membrane component was actually a beta-glucosidase, coupled to an energy-dependent transport system for the glucose moiety; the function of the latter was rate-limiting in the over-all activity of the entire system.
J Gen Physiol 1966 Sep
PMID:The beta-glucosidase of the yeast cell surface. 597 Oct 36

1. Culture filtrates from Trichoderma viride have been fractionated by gel filtration on Sephadex G-75 followed by ion-exchange chromatography on DEAE- and SE-Sephadex. 2. The components essential for attack on cotton are a carboxymethylcellulase, a cellobiase and a third (C(1)) component which has no action on CM-cellulose, cellobiose or cotton. 3. These components, which together can completely convert cotton into water-soluble products, lose this ability when separated and regain it quantitatively when recombined in their original proportions.
Biochem J 1967 Sep
PMID:The cellulase of Trichoderma viride. Separation of the components involved in the solubilization of cotton. 606 3

Activities of certain acid hydrolases (viz. acid phosphatase, beta-glucosidase, beta-galactosidase, N-acetyl-beta-D-glucosaminidase and cathepsine) of post mitochondrial fraction of liver and spleen were studied during the course of Dipetalonema viteae infection in Mastomys natalensis. The values are significantly higher from prepatent to patent phase of infection as compared with normal animals. However, a decrease in the activity of hepatic acid phosphatase and N-acetyl-beta-D-glucosaminidase was noticed in latent phase of infection while a several fold increase in the activity of these enzymes was observed in splenic tissue when there were no detectable microfilariae (mf) in peripheral circulation. The results suggest that lysosomal acid hydrolases which constitute an important component of resistance may be activated by mf products through the sensitized cells of RE system.
Tropenmed Parasitol 1983 Sep
PMID:Lysosomal enzyme in Mastomys natalensis during Dipetalonema viteae infection. 641 75

The enzyme activity of the rat hindgut microflora maintained in an anaerobic two-stage continuous culture was compared with that of rat cecal contents. A qualitative comparison (API ZYM) showed a high degree of similarity between the two populations. Quantitative determinations showed that azoreductase, beta-glucosidase, nitrate reductase, and nitroreductase activities were comparable, and that beta-glucuronidase activity was very low in the culture. beta-Glucuronidase, beta-glucosidase, and nitrate reductase activities were induced within the culture by their respective substrates. Bile acids influenced microbial activity in vitro, with cholic acid inducing beta-glucosidase, azoreductase, and beta-glucuronidase activities and decreasing nitrate reductase activity. Chenodeoxycholic acid increased beta-glucosidase and beta-glucuronidase activities and decreased azoreductase, nitrate reductase, and nitroreductase activities in vitro. These studies demonstrate that the rat hindgut microflora may be successfully cultured in vitro and suggest control mechanisms that regulate the metabolic activity of these organisms in vivo.
Appl Environ Microbiol 1983 Sep
PMID:Metabolic activity and enzyme induction in rat fecal microflora maintained in continuous culture. 641 66

Mouse peritoneal macrophages that had been treated with a monovalent carboxylic ionophore, monensin, selectively secreted lysosomal and nonlysosomal granular enzymes into the medium. When macrophages were incubated with 1 to 10 microM monensin, the release of beta-glucuronidase, beta-hexosaminidase and beta-galactosidase was stimulated time and does dependently. Neither the beta-glucosidase nor acid phosphatase, enzymes bound to the lysosomal membranes, however, were released by monensin. Neutral alpha-glucosidase, shown recently to be localized in nonlysosomal granules of macrophages (15), was released by monensin at concentrations lower than those required for lysosomal enzyme release. Increased release of lysosomal enzymes also took place in a manner similar to that seen with monensin-treated macrophages after treatment of macrophages with weak bases, chloroquine and ammonium chloride. Neutral alpha-glucosidase, however, was not released when chloroquine was present in concentrations that stimulated the release of lysosomal enzymes. The UDP-galactosyltransferase activity of the Golgi apparatus in the macrophages markedly decreased after treatment with low concentration of monensin.
Cell Struct Funct 1984 Sep
PMID:Stimulation of the release of lysosomal and nonlysosomal granular enzymes from macrophages treated with monensin. 643 21

The ultrastructural localization of four acid hydrolases (acid phosphatase, beta-glucuronidase, beta-glucosaminidase and alpha-naphthylacetate esterase) has been studied in lymphocytes from 16 patients with three types of chronic T-cell leukaemia, namely, T-prolymphocytic leukaemia (T-PLL), T-chronic lymphocytic leukaemia (T-CLL) and adult T-cell lymphoma leukaemia (ATLL). Different patterns of enzyme distribution were observed in the leukaemic T-cells from these disorders. In T-PLL, reactivity for the four acid hydrolases was confined to single or a few large granules. Gall bodies were reactive for beta-glucuronidase, b-glucosaminidase and alpha-naphthylacetate esterase but apparently unreactive for acid phosphatase. In T-CLL, scattered small- to medium-size cytoplasmic granules and many parallel tubular arrays were strongly reactive for acid phosphatase, beta-glucuronidase and beta-glucosidase but showed no reactivity for alpha-naphthylacetate esterase. Intermediate features were observed in ATLL. The observed differences in enzyme reactivity reflect a different content of lysosomal granules in the various types of leukaemic T-cells. They also suggest that similar differences may be found in normal T-lymphocyte subsets.
Histochem J 1983 Sep
PMID:Ultrastructural cytochemistry of chronic T-cell leukaemias. A study with four acid hydrolases. 660 30

The API STAPH-IDENT system was compared with conventional methods for the identification of 14 Staphylococcus species. Conventional methods included the Kloos and Schleifer simplified scheme and DNA-DNA hybridization. The API STAPH-IDENT strip utilizes a battery of 10 miniaturized biochemical tests, including alkaline phosphatase, urease, beta-glucosidase, beta-glucuronidase, and beta-galactosidase activity, aerobic acid formation from D-(+)-mannose, D-mannitol, D-(+)-trehalose, and salicin, and utilization of arginine. Reactions of cultures were determined after 5 h of incubation at 35 degrees C. Results indicated a high degree of congruence (greater than 90%) between the expedient API system and conventional methods for most species. The addition of a test for novobiocin susceptibility to the API system increased the accuracy of identification of S. saprophyticus, S. cohnii, and S. hominis, significantly. Several strains of S. hominis, S. haemolyticus, and S. warneri which were difficult to separate with the Kloos and Schleifer simplified scheme were accurately resolved by the API system.
J Clin Microbiol 1982 Sep
PMID:Identification of Staphylococcus species with the API STAPH-IDENT system. 675 90

Quantitative high-performance liquid chromatographic analysis of perbenzoylated sphingolipids has been used to study the correlations of body chemistry to clinical phenomena. Plasma sphingolipids were isolated from 32 Gaucher (beta-glucosidase deficiency) and six Fabry (alpha-galactosidase deficiency) patients by solvent partition and chromatographic separation on silicic acid columns. Plasma sphingolipids from a patient undergoing plasma-exchange were separated from interfering lipids with reversed-phase columns. Liquid-chromatographic analysis of sphingolipids provides useful supportive information for diagnoses because affected individuals are shown to possess increased circulating concentrations of the pathognomonic sphingolipid. We also used this technique to monitor sphingolipid concentrations in plasma and urine sediment during plasma exchange of a p atient with Fabry's disease. Regular plasma exchanges produced and maintained decreased concentrations of sphingolipids in plasma, but near pre-exchange concentrations were observed within days after the therapy was terminated.
Clin Chem 1980 Sep
PMID:Application of "high-performance" liquid chromatography to the study of sphingolipidoses. 677 1

To date, enzymatic diagnosis of Gaucher's disease via a fluorometric assay procedure which utilizes 4-methylumbelliferyl-beta-D-glucopyranoside as a substrate has not been possible when liver serves as the source of enzyme since currently employed fluorometric procedures cannot adequately differentiate between a broad-specificity beta-glucosidase and lysosomal glucocerebrosidase activities in crude extracts of liver. Incorporation of conduritol-beta-epoxide into the incubation medium for the fluorometric assay allows one to selectively measure the glucocerebrosidase activity present in a given liver extract. In five cases of Gaucher's disease this revised fluorometric procedure proved as effective as the assy procedure which utilizes authentic, radiolabeled glucocerebroside as the substrate in demonstrating a deficiency of glucocerebrosidase activity in liver.
Clin Chim Acta 1980 Sep 25
PMID:A revised fluorometric assay for Gaucher's disease using conduritol-beta-epoxide with liver as the source of Beta-glucosidase. 677 4

Leukocytes were isolated from 14 patients (7 males and 7 females ) with Gaucher disease of the Norrbottnian type (Type 3), 32 obligate heterozygotes (16 males and 16 females) for this disease and 20 controls (10 males and 10 females). After collection, the cells were transported in dry ice to the laboratory, where they were assayed. The assays were repeated after the cells had been stored for 12 months. beta-Glucosidase activity was assayed with D-[glucose-U-14C]glucosylceramide at pH 5.8 with Cutscum-Na-cholate as a detergent and 4-methylumbelliferyl-beta-glucoside at pH 4.1 with Triton-Na-taurocholate as a detergent. The activities of two marker enzymes, 4-methylumbelliferyl-beta-galactosidase and N-acetyl-beta-glucosaminidase, were assayed in aliquots of the same leukocyte samples. The activity of beta-galactosidase remained constant during storage, N-acetyl-beta-glucosaminidase increased, while beta-glucosidase decreased as assayed with the natural as well as with the artificial substrate. beta-Glucosidase activity was significantly lower in the female than in male controls and heterozygotes. When assayed with natural substrate beta-glucosidase activity in leukocytes from the male patients was 6--12% of the control mean value and 10--15% in those from the female patients. The corresponding figures found when the artificial substrate was used were 15--30% and 22--45%. The values for the heterozygotes were respectively 42--68% and 34--79% with the natural substrate, and 33--82% and 51--109% with the artificial substrate. No correlation was found between the age of the patient and the beta-glucosidase activity.
Clin Chim Acta 1980 Sep 25
PMID:Assay of the beta-glucosidase activity with natural labelled and artificial substrates in leukocytes from homozygotes and heterozygotes with the Norrbottnian type (Type 3) of Gaucher disease. 677 5


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>