Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

At 20 degrees C, aflatoxin B1, at a sublethal dose, decreases the activity of alkaline phosphatase (EC 3.1.3.1), alpha-glucosidase (EC 3.2.1.20), esterase (EC 3.1.1.1), chymotrypsin (EC 3.4.21.1), leucine aminopeptidase (EC 3.4.11.1), and phosphoamidase (EC 3.9.1.1) biosynthesis in Bacillus thuringiensis (Berliner). In contrast, at 41 degrees C no significant decrease was observed. At this temperature, the mycotoxin is not destroyed or metabolized and bacterial cells are resistant to the toxin.
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PMID:[Effect of aflatoxin B1 on the enzymatic activities of Bacillus thuringiensis (Berliner)]. 88 28

In recent years the hypothesis that the number of villus cells regulates crypt cell proliferation in the epithelium of the small intestine has been brought forward by a number of investigators. To test this hypothesis, the villus cell population was reduced by clamping the superior mesenteric artery and vein in rats for 1 hr and the effects on the intestinal epithelium were studied during the first 24 hr. It was shown that temporary interruption of the blood flow to the small intestine led to a marked decrease in the number of functional villus cells within 2 hr; preferentially, cells from the upper part of the villus were lost and the number of crypt cells was not affected. This reduction in the number of villus cells led to an increase in the percentage of labeled crypt cells after pulse labeling with [3H]thymidine, and an expansion of the proliferative cell compartment in the crypt. After a peak of proliferative activity at 16 hr, the investigated crypt cell kinetic parameters approached control values after 24 hr, as did the number of villus cells. The enzyme activities of nonspecific esterase and neutral alpha-glucosidase showed marked decreases in isolated crypt and villus cell compartments as crypt cell proliferation increased. These data support the view that the feedback control of crypt cell proliferation by the functional villus cells, and confirm earlier data on the influence of changing cell kinetics on crypt cell maturation. Additional data which were obtained after creating temporary ischemia in part of the small intestine support the hypothesis of a feedback control of crypt cell proliferation by the functional villus cells, and confirm earlier data on the influence of changing cell kinetics on crypt cell maturation. Additional data which were obtained after creating temporary ischemia in part of the small intestine support the view that the feedback control of proliferation by the villus cells is a local control mechanism.
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PMID:The effect of ischemic villus cell damage on crypt cell proliferation in the small intestine: evidence for a feedback control mechanism. 96 70

Initiated by the recently published histochemical method for the investigation of alfa-D-galactosidas with an indoxyl substrate, the current state of this group of synthetic compounds in light and electron microscopic histochemical glycosidase research is evaluated whereby historical, functional, methodological and applied aspects are considered. Beginning with the introduction of indoxyl acetate for non-specific esterase in 1951 and 1952 numerous other indoxyl substrates and mostly substituted in the 5- and 4-position of the indol ring by Br and Cl were developed to study histochemically non-specific phosphatases and glycosidases and frequently used in indigogenic, azoidoxyl, tetrazolium salts and metal salt techniques for catalytic (activity) histochemical and less often for immunohistochemical, affinity histochemical and hybridohistochemical purposes. The last substrate which became available and was validated for activity histochemistry was 5-Br-4-Cl-3-indoxyl alfa-1-galactoside for alfa-1-galactosidase. At present, the indoxyl glycosides are more widely used than 5-Br-4-Cl-3-indoxyl acetates and phosphates when compared with the alternative synthetic (artificial) naphthol, 6-Br-2-naphthol or ternative synthetic (artificial) naphthol, 6-Br-2-naphthol AS substrates, and among the indoxyl glycosides those for the oxoglycosidases lactase, maltase-glucoamylase, glucoamylase, acid beta-D-galactosidase, neuroaminidase and alfa-D-galactosidase are superior to other artificial compounds. When one considers in addition, electron microscopic catalytic glicosidase histochemistry (ultracytochemistry, 5-Br-4-Cl-3-indoxyl is the only suitable moiety for this purpose. These glycosidase can mostly be localized in plasma membranes or lysosomes and also measured there in tissue sections but are also found in secretion granules, endoplasmic reticulum and organ lumina.
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PMID:Indoxyl alfa-D-galactoside as the temporarily last substrate for glycosidase histochemistry. The present state of the art in histochemical glycosidase research using indoxyl glycosidas. 209 81

Cells of Entamoeba histolytica grown over a period of four days contained NADP+-dependent alcohol dehydrogenase exclusively inside the cells. No activity of this enzyme could be found in the growth medium after harvesting the cells. Under the same conditions, acid phosphatase, beta-N-acetylglucosaminidase, esterase, alpha-glucosidase, and different amylases of the parasite were found both inside the cells and in the medium. The activities present in the cell homogenate and in the medium before and after growth of the amoebas were partially separated by gel filtration on Sephadex G150 and G75, respectively. The comparison of the elution diagrams revealed that NADP+-dependent alcohol dehydrogenase, acid phosphatase, esterase, and amylases occurred as multiple forms inside the cells. These activities, as well as beta-N-acetylglucosaminidase and alpha-glucosidase, were released into the extracellular environment to a different degree. The enzymes originating from the parasite were identified and distinguished from those of the ingredients of the growth medium according to their molecular mass and pH optimum. Furthermore, the amoebic origin of the secreted enzymes was shown on the basis of their inhibition by antibodies prepared against the supernatant fraction of the homogenate.
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PMID:Secretory hydrolases of Entamoeba histolytica. 245 86

Since they are found to be increased in lesions of acute necrotic ulcerative gingivitis or marginal periodontitis, agents for these diseases. In the present study, 38 pure cultured strains were obtained as a result of isolation and culture of samples collected from lesions of marginal periodontitis (periodontal pokets), and the biological and biochemical characteristics of these strains were investigated. 1) Light microscopy (including dark-field microscopy) and transmission electron microscopy (negative staining) were used for observation of the morphology and cellular structure of the strains. The cells had a spiral shape, and showed active movement. Based on the above findings the cultured strains were all confirmed to be spirochetes of small to medium size, being 0.08-0.24 micron in width. 2) Growth and motility of the strains were investigated on various types of culture medium. Intense growth and movement were noted in strains cultured in bovine liver exudate medium containing horse serum (pH 7.2) at 37 degrees C under anaerobic conditions produced by the evacuation-replacement method (95% N2, 5% CO2) for 3-7 days after inoculation. 3) Thirty-five strains were positive for indole production and decomposition of urea, mucin, hippuric acid and esculin. Production of hydrogen sulfied was observed in 31 strains. In decomposition tests for 17 carbohydrates, 17 strains were positive for galactose and 14 strains were positive for glucose, while 11 strains were positive for dextrin and 10 strains for fructose upon decomposition of soluble starch. Other carbohydrates were also decomposed by a few strains. 4) In an investigation of the production of alcohol and lower fatty acids, among the metabolic products detected by gas chromatography, a large amount of acetic acid and small amounts of ethanol, lactic acid, propionic acid, pyruvic acid were observed. 5) The results of enzyme activity tests using an API ZYM system indicated relatively high activities of esterase, esterase-lipase, alpha-glucosidase, alkaline phosphatase, trypsin and acid phosphatase.
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PMID:[Biological and biochemical characteristics of the oral spirochetes isolated from the focus of marginal periodontitis]. 276 48

The enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.
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PMID:Enzymatic characterization of Pseudomonas cepacia by API ZYM profile. 335 98

Nineteen hydrolytic enzymes were detected in individual adult Pergamasus longicornis (Berlese) mites--amylase, hide protease, alkali phosphatase, esterase (C4), esterase lipase (C8), lipase (C14), leucine arylamidase, valine arylamidase, cystine arylamidase, acid phosphatase, phosphoamidase, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, beta-glucosidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase, and alpha-fucosidase. All but the phosphatases were detected for the first time. Tryptic and chymotryptic activity were consistently not demonstrable. Comparisons are made with saprophagous mites. No clear enzymic specialization for predation was found.
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PMID:Digestion in the soil predatory mite Pergamasus longicornis (Berlese) (Acari: Mesostigmata: Parasitidae)--detectable hydrolases. 356 25

The aim of our presentation was to show how we characterize cells cultured in monolayer system. Cytological and biochemical methods were used. Ovarian Krukenberg tumour fibroblasts were investigated and findings were correlated with normal human diploids (HDZ1) and with fibroblasts obtained from Blighted ovum. Cytomorphologically Malignancy associated changes in the tumour fibroblasts were found. Cytochemically acid phosphatase and alpha-naphtyl-esterase were positive (+++). PAS reaction was doubled in 18th passage. Cytogenetically normal human diploids were found. Biochemically enzymatic assay showed phosphopentose shunt is decreased in tumour fibroblasts and alpha-glucosidase and beta-galactosidase activities were significantly lower in these cells. A form of N-acetyl-beta-glucosaminidase fell during the investigation from normal 75% to lower percent (42% of the total activity). Much more parameters were obtained by different methods and Krukenberg tumour fibroblasts may be better understood. In vitro investigation makes a contribution to biomedical knowledge in cancer research.
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PMID:Cytological and biochemical methods for the characterization of in vitro cultured cells. 626 64

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

The present study was performed to investigate the enzymatic changes in dystrophic chickens compared to those of dystrophic mice. The activities of 14 kinds of aminopeptidases, 5 kinds of endopeptidase, 4 kinds of glycosidases, phosphatase, esterase, and ribonuclease were measured in muscles of control and dystrophic chickens. When the enzyme activities were expressed as specific activity per unit weight of organs, only some of them were found to be significantly elevated in dystrophic chickens; e.g., alanine aminopeptidase (Ala-AP), Gly-AP and cathepsin D. On the contrary, the activities of alpha-D-glycosidase, alpha-D-galactosidase and alpha-D-mannosidase were significantly decreased. Muscular protein contents of dystrophic chickens also tended to be lower than those of controls. These observations offer a striking contrast with the one obtained in the study on dystrophic mice. However, when expressed as specific activity per mg protein, many enzyme activities were found to be significantly elevated suggesting an extensive abnormality of metabolism in dystrophic chickens. Among 14 kinds of aminopeptidase activities, highly significant elevations were seen especially in AP-A, AP-B, Gly-AP, Ala-AP, Ser-AP, Pro-AP, Leu-AP, Met-AP and Trp-AP. Interestingly enough, a statistical approach suggested a significant correlation between the aminopeptidase changes of dystrophic chickens with those of dystrophic mice. In addition to aminopeptidases, there were highly significant increases in the activities of cathepsin D, alpha-D-glucosidase, beta-D-galactosidase, alpha-D-mannosidase, esterase and RNase. These results indicate that the intramuscular metabolic abnormality of dystrophic chickens are generally different from but partly resembled with those of dystrophic mice.
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PMID:Intramuscular enzyme abnormalities of dystrophic chickens compared to those of dystrophic mice. 701 13


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