Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Target Concepts:
Gene/Protein
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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 comparison with 1- and 2-naphthyl beta-D-glucoside, beta-D-galactoside, beta-D-glucuronide, beta-D-N-acetylglucosaminide, alpha-D-glucoside, alpha-D-galactoside and alpha-D-mannoside 1- and 2-naphthyl alpha-L-fucoside are hydrolyzed more quickly or to the same extent by homogenates prepared from freeze-dried cryostate sections of various rat organs. Nevertheless, when the fucosides are employed for the histochemical demonstration of alpha-L-fucosidase mostly negative data were obtained independent on the method used, whereas all other naphthyl glycosies deliver positive results. The reasons for these discrepancies are the marked inhibition of alpha-L-fucosidase by aldehyde fixation and diazonium salts. Then, alpha-L-fucosidase activity is suppressed to 90% and between 85 and 98% respectively; the inhibition of alpha- and
beta-D-glucosidase
, alpha- and beta-D-
galactosidase, alpha
-D-mannosidase, beta-D-glucuronidase and beta-D-N-acetylglucosaminidase by the fixative or coupling reagent does not exceed 70%. Therefore 1- and 2-naphthyl alpha-L-fucoside cannot be recommended in general for histochemical purposes. Small amounts of dimethylformamide do not influence the activity of most of the glycosidases investigated. For biochemical measurements, however, especially 1-naphthyl alpha-L-fucoside represents a suitable alternative in a fluorometric procedure instead of p-nitrophenyl alpha-L-fucoside used for the photometric evaluation of alpha-L-fucosidase. With the fluorometric method the enzyme was measured in rat organs, which posses remarkably different activities of alpha-L-fucosidase.
...
PMID:[Suitability of naphthyl-alpha-L-fucosides for the investigation of alpha-L-fucosidases (author's transl)]. 88 38
The circadian and circannual group rhythms in the plasma concentrations of the following lysosomal enzymes were studied in women and men: beta-D-N-acetylglucosaminidase, beta-D-glucuronidase,
beta-D-glucosidase
, beta-D-
galactosidase, alpha
-D-
galactosidase, alpha
-L-fucosidase and alpha-D-mannosidase. The circadian rhythm was detected in all the tested enzymes of women, and only in alpha-D-galactosidase,
beta-D-glucosidase
, alpha-D-mannosidase and beta-D-N-acetylglucosaminidase of men. A statistically significant difference between genders in the circadian rhythm was exhibited by beta-D-galactosidase,
beta-D-glucosidase
, beta-D-N-acetylglucosaminidase, beta-D-glucuronidase, alpha-D-galactosidase and alpha-L-fucosidase. A circannual rhythm was detected in all the tested enzymes, with the exception of beta-D-glucuronidase and beta-D-N-acetylglucosaminidase, without any statistically significant difference between genders. The group rhythms of some of the enzymes (alpha-D-galactosidase,
beta-D-glucosidase
, beta-D-galactosidase) showed similar values of both circadian and circannual acrophases, suggesting that they may be subjected as a group to the same chronobiological coordination. The chronobiological rhythms of lysosomal enzymes were different from those of lactate dehydrogenase and alpha 1-antitrypsin, indicating that these rhythms are not merely reflecting fluctuations of the water content of plasma. No in-phase relationship was observed between the circadian and circannual rhythms of plasma cortisol and those of the tested lysosomal enzymes, excluding a direct chronobiological relationship between this hormone and lysosomal enzymes.
...
PMID:Circadian and circannual rhythms of several enzymes of lysosomal origin in human plasma. 313 30
Assay conditions were studied for eleven lysosomal enzymes (beta-D-
galactosidase, alpha
-D-mannosidase, beta-hexosaminidase, beta-D-glucuronidase, alpha-D-galactosidase, alpha-D-glucosidase, arylsulfatase,
beta-D-glucosidase
, alpha-L-fucosidase, alpha-D-neuraminidase and alpha-L-iduronidase) in cultured amniotic fluid cells (CAFC), cultured skin fibroblasts (CSF) and cultured embryonic lung fibroblasts (CELF), and the properties of the enzymes were compared among these cultured cells. In addition, changes in these enzymes from the three cell types were investigated between 4-6 earlier passages and 24-26 later passages. With the exception of alpha-D-glucosidase, alpha-D-neuraminidase and alpha-L-fucosidase, all enzymes assayed for the 4-6 earlier passages and the 24-26 later passages had the same Km values and the same pH optima, and were also unchanged with the increasing age of cell cultures, with regard to their points. The specific activities of beta-D-glucuronidase, arylsulfatase, alpha-D-glucosidase and
beta-D-glucosidase
for the 4-6 earlier passages increased significantly with development, though no change was observed with development in the specific activities of other enzymes. Variations were observed between the levels of these enzymes in the three cell types with the increasing age of cell cultures, such as increases in some, decreases in others and no change in still others.
...
PMID:Comparative enzymology of eleven acid hydrolases in cultured amniotic fluid cells, skin fibroblasts and embryonic lung fibroblasts, and the respective changes with the increasing age of the cell cultures. 316 Dec 15
Several lysosomal enzymes (beta-N-D-acetylglucosaminidase, beta-D-glucuronidase, alpha-D-galactosidase, beta-D-
galactosidase, alpha
-L-fucosidase, alpha-D-glucosidase, alpha-D-mannosidase,
beta-D-glucosidase
), glycated albumin and glycated hemoglobin (HbA1c) were determined in the serum of 81 insulin-dependent diabetics with different degrees of metabolic control (optimal, 21 patients; good, 39 patients; poor, 21 patients) and without signs of complications, and in 42 control subjects. All parameters examined increased in serum in inverse proportion to the degree of metabolic control. A highly significant correlation (p less than 0.01) was found between lysosomal enzymes and both glycated albumin and HbA1c. All parameters correlated with hyperglycemia, glycated albumin having the highest r-value (0.586) and lysosomal enzymes the lowest one. Unlike glycated albumin and HbA1c, serum levels of lysosomal enzymes in patients with optimal metabolic control were undistinguishable or even lower than those of controls. A 2-month longitudinal monitoring of a patient who was hospitalized in conditions of poor metabolic control and adequately treated, proved that lysosomal enzymes diminished in serum parallel to glycated albumin and HbA1c in relation to improvement of the metabolic situation. The conclusion is drawn that serum lysosomal enzymes are good indicators of the metabolic control of diabetic patients probably reflecting the overall metabolic state connected with insulin action rather than hyperglycemia.
...
PMID:Serum enzymes of lysosomal origin as indicators of the metabolic control in diabetes: comparison with glycated hemoglobin and albumin. 375 46
Some glycosidase activities have been determined in blood sera from 21 patients who ingested a toxic oil (rapeseed oil denatured with aniline(s) and treated by a thermal process). The samples were collected from the same patients on 3 or 4 occasions during a period of 11-12 mth. During this period, the clinical state of the patients improved and, generally, they were restored to health. beta-N-Acetylglucosaminidase, alpha-L-fucosidase, beta-D-glucuronidase,
beta-D-glucosidase
and alpha-D-mannosidase activities, which were higher in patients than in 17 controls during the first mth decreased to normal values in the period studied, 11-12 mth. In contrast, beta-D-
galactosidase, alpha
-D-galactosidase and alpha-D-glucosidase activities, which were initially lower in patients than in controls, were finally similar or higher than in controls. One explanation for these results could be the possible alteration of the cell membrane(s) by the toxic substance(s).
...
PMID:Glycosidase activities in sera from convalescent patients who ingested a toxic oil. 398 46
Fluorescent Pseudomonas species (P. aeruginosa, P. fluorescens, P. putida) were tested for the presence of glycosidase activities (alpha-D-glucosidase,
beta-D-glucosidase
, alpha-D-galactosidase, beta-D-galactosidase, beta-xylosidase, alpha-D-mannosidase, alpha-L-fucosidase, beta-L-fucosidase, beta-D-glucuronidase and N-acetyl-beta-D-glucosaminidase). Some of the investigated glycosidases were always absent, while N-acetyl-beta-D-glucosaminidase was constantly present in all strains; 3 glycosidase activities were observed in association or separately. Serotype O11 of P. aeruginosa was found to be homogeneous with respect to some of those enzymatic activities. Search for beta-D-
galactosidase, alpha
-D-glucosidase and
beta-D-glucosidase
may be of diagnostic value in epidemiologic studies of P. aeruginosa.
...
PMID:[Detection of glycosidases in Pseudomonas of the fluorescent group: relation between serotype and glycosidase activities in P. aeruginosa]. 642 62
Some hydrolytic enzyme activities, mainly typical of lysosomal localization, have been determined in blood sera from patients who ingested a rapeseed oil (denatured with anilines and treated by a thermal process), and in healthy subjects. beta-N-Acetylglucosaminidase,
beta-D-glucosidase
, beta-D-glucuronidase, alpha-L-fucosidase and leucine aminopeptidase activities were significantly higher when compared with controls (p less than 0.001); higher activities but not significant (p less than 0.2) differences were found for alpha-D-mannosidase and alkaline phosphatase. In contrast, beta-D-
galactosidase, alpha
-D-galactosidase, acid phosphatase and lipase showed lower activities than controls. The significance of these results is discussed.
...
PMID:Hydrolytic enzyme activities, mainly from lysosomal localization, in sera from patients who ingested a toxic oil. 683 4
The current study reports active glycosidases in the lens of ICR/f rats, which generate a hereditary cataract approximately 90 d after birth, and the variation in enzyme activity with cataract progression. Seven active glycosidases, beta-D-
galactosidase, alpha
-D-glucosidase, beta-D-glucosidase, beta-D-glucuronidase, beta-D-galactosaminidase, beta-D-glucosaminidase and alpha-D-mannosidase, were detected in ICR/f rat lenses. Of these, beta-D-glucuronidase and beta-D-galactosidase showed a tendency to increase in activity with the cataract progression. Furthermore,
beta-D-glucosidase
and alpha-D-mannosidase showed a transitory increase in activity at the time of cataract formation. This result suggests that several glycosidases in the lens may be involved in the hereditary cataract formation. The optimal pH and temperature of the seven active glycosidases in rat lenses were also measured in this study.
...
PMID:Variation in glycosidase activity in soluble fractions in ICR/f rat lenses with the progression of cataract formation. 1007 42
The erythrocyte membrane in 71 patients with type 2 diabetes mellitus was assessed for glycohydrolase activity: N-acetyl-beta-D-glucosaminidase, beta-D-glucuronidase, alpha- and beta-D-
galactosidase, alpha
- and
beta-D-glucosidase
, alpha-D-mannosidase, and alpha-L-fucosidase. Only beta-D-glucuronidase, alpha-D-glucosidase, and
beta-D-glucosidase
showed markedly elevated levels with respect to the controls regardless of the presence of complications. Among the examined patients, those with good metabolic control (not yet submitted to any therapy) showed the same enzyme levels as the reference subjects, while the levels in patients with unsatisfactory metabolic control (treated with oral hypoglycemic and/or insulin) significantly differed from the control levels. For alpha-D-glucosidase and
beta-glucosidase
, a correlation with glycemia and the parameters of metabolic control was also evidenced. Alterations of beta-D-glucuronidase, alpha-D-glucosidase, and
beta-D-glucosidase
were also ascertained in the plasma of the same diabetic patients according to the literature; each enzyme correlated with the other, either in plasma or in the erythrocyte membrane. This study shows a correlation between plasma and erythrocyte membrane levels for these three enzymes. The strict parallelism of the glycohydrolases in the two different compartments provides a profile of these enzymes in the pathology of diabetes.
...
PMID:Alterations in the activity of several glycohydrolases in red blood cell membrane from type 2 diabetes mellitus patients. 1042 Dec 18
Investigation of 15 different glycoside activities of 64 strains isolated from water and invertebra of the Black Sea has shown that 64% of the studied strains displayed the capacity to synthesize enzymes with alpha-L-ramnosidase activity which varied from 0.01 to 0.20 un/ml depending on the strain. The greatest number of the enzyme producers was found in representatives of Alteromonas macleodii. Other investigated glycosidase activities: alpha-amylase, beta-N-acetyl-D-glucosaminidase, beta-D-glucuronide, alpha-N-acetyl-D-galactosaminidase, beta-N-acetyl-D-galactosaminidase, beta-D-
galactosidase, alpha
-D-galactosidase,
beta-D-glucosidase
, KM-cellulase activities though have been found, but mainly with inconsiderable indices, alpha-D-glucosidase, alpha-D-mannosidase, alpha-L-fucosidase, beta-D-xylosidase and alpha-D-xylosidase activities were found in neither of the studied strains. Strains with rather high proteolytic activity were found among marine species of bacteria. It has been established that 18 strains (28%) of 64 marine isolates were characterized by rather high level of total proteolytic activity (from 0.1 to 05 un/ml), 43.75% of them displayed inconsiderable (up to 0.1 un/ml) or only trace (up to 0.01 un/ml), 18.75% did not display any hydrolytic activity in respect of casein. Investigation of substrate specificity to a number of fibrillar and globular proteins of 9 studied strains, which displayed considerable general (caseinolytic) activity has shown that 8 of them displayed fibrinolytic activity from 0.15 to 2.175 un/ml. All 9 strains were characterized by gelatin activity. Collagenase and keratinase activity was also revealed. Neither of 9 studied strains displayed elastase activity.
...
PMID:[The Black Sea bacteria--producers of hydrolytic enzymes]. 2216 94
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