scholarly journals Specific inactivation of lysosomal glycosidases in living fibroblasts by the corresponding glycosylmethyl-p-nitrophenyltriazenes

1980 ◽  
Vol 188 (2) ◽  
pp. 337-343 ◽  
Author(s):  
O P Van Diggelen ◽  
H Galjaard ◽  
M L Sinnott ◽  
P J Smith
Keyword(s):  
Cell Viability ◽  
Enzyme Production ◽  
Zero Order ◽  
Fibroblast Cultures ◽  
Beta Glucosidase ◽  
Alpha Glucosidase ◽  
Beta Galactosidase ◽  
Lysosomal Glycosidases

1. beta-D-Galactopyranosylmethyl-p-nitrophenyltriazene can specificag detectable changes in cell viability or the activities of other hydrolases. 2. beta-D-Glucopyranosylmethyl-p-nitrophenyltriazene behaves similarly towards lysosomal beta-glucosidase, but also inactivates some alpha-glucosidase. 3. Both beta-galactosidase and beta-glucosidase activities in triazene-treated confluent fibroblast cultures recover exponentially; if zero-order enzyme production is assumed, turnover times of 10 and 5 days respectively can be estimated.

scholarly journals Effects of a probiotic in combination with prebiotics on intestinal lactobacilli and coliforms and activities of bacterial enzymes in 1,2-dimethylhydrazine exposed rats

2011 ◽  
Vol 56 (No. 3) ◽  
pp. 99-106 ◽  
Author(s):  
L. Strojný ◽  
A. Bo ◽  
E. Hijová ◽  
A. Chmelárová ◽  
G. Mojžišová ◽  
...  
Keyword(s):  
High Fat Diet ◽  
Control Group ◽  
Group 4 ◽  
Group 3 ◽  
Group 5 ◽  
Group 2 ◽  
Beta Glucosidase ◽  
Alpha Glucosidase ◽  
Beta Galactosidase ◽  
Group 1

Effects of the probiotic (PRO) Lactobacillus plantarum and of the combination of PRO and the prebiotic (PRE) inulin enriched with oligofructose (2%), and PRO with Lini oleum virginale (O) on counts of lactobacilli and coliforms and enzymatic activities in faeces of rats were studied. The rats (n = 60) were divided into 5 groups of 12 subjects. The animals were fed on a high fat diet (10%) for 8 weeks of experiment. Colon cancer was induced by the application of 1,2-dimethylhydrazine (DMH) twice a week in a dose of 20 mg/kg s.c. in groups G2-G5. The rats in group 1 (control 1) received a diet without any supplements. The rats in group 2 (control 2) received 1,2 DMH without any supplements. The rats in group 3 received PRO, group 4 PRO and PRE, and group 5 received PRO and O. A significant decrease (P < 0.05) of coliforms was found out after the application of PRO, PRO-O, and PRO-PRE in comparison with control group G2. Significantly higher (P < 0.05) counts of lactobacilli were determined after the application of PRO-O and PRO-PRE. Significantly lower (P < 0.001) activities of β-galactosidase, β-glucuronidase and α-glucosidase were observed in PRO, PRO-PRE and PRO-O, while in the case of the enzyme β-glucosidase the activity was lower only after the addition of PRO-O. The protective effect of lactobacilli was observed in the order PRO-O, PRO-PRE, and PRO. It was shown that combinations of PRO-O and PRO-PRE had a synergistic effect which was higher than the effect of administering only PRO.

scholarly journals Functional lysosomal hydrolase size as determined by radiation inactivation analysis

1985 ◽  
Vol 226 (1) ◽  
pp. 283-288 ◽  
Author(s):  
G Dawson ◽  
J C Ellory
Keyword(s):  
Target Size ◽  
Lysosomal Hydrolase ◽  
Lysosomal Hydrolases ◽  
Range Analysis ◽  
Freeze Dried ◽  
Arylsulphatase A ◽  
Alpha Galactosidase ◽  
Beta Glucosidase ◽  
Alpha Glucosidase ◽  
Beta Galactosidase

Electron inactivation analysis with 16 MeV electrons was used to determine the functional target size of a number of commonly studied lysosomal hydrolases. Observed values ranged from a low of 62 000 +/- 4000 Da for beta-galactosidase to a high of 200 000 +/- 17 500 Da (mouse beta-glucuronidase). One group of lysosomal hydrolases (N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, alpha-galactosidase, beta-mannosidase, beta-glucosidase, arylsulphatase A and sphingomyelinase) had target sizes in the range 100 000-120 000 Da, whereas alpha-glucosidase and alpha-fucosidase exist as complex multimers in the 150 000-160 000 Da range. Analysis of freeze-dried cell material showed little evidence of species (mouse versus human) variation in the functional size of most lysosomal hydrolases with the exception of beta-glucuronidase. Our findings suggest the potential usefulness of lysosomal hydrolases as endogenous marker enzymes in studies where the target size of proteins of unknown molecular mass is to be determined.

scholarly journals Soil hydrolase activities and kinetic properties as affected by wheat cropping systems of Northeastern China

2010 ◽  
Vol 56 (No. 11) ◽  
pp. 526-532 ◽  
Author(s):  
Y.L. Zhang ◽  
L.J. Chen ◽  
C.X. Sun ◽  
Z.J. Wu ◽  
Z.H. Chen ◽  
...  
Keyword(s):  
Cropping Systems ◽  
Reaction Rates ◽  
Total Carbon ◽  
Kinetic Properties ◽  
Total N ◽  
Alpha Galactosidase ◽  
Beta Glucosidase ◽  
Alpha Glucosidase ◽  
Beta Galactosidase ◽  
Sequential Cropping

Agricultural practices that reduce soil degradation and improve agriculture sustainability are important particularly for dry hilly land of Chaoyang County in the Liaoning Province, North-east China, where cinnamon soils are widely distributed and mainly for wheat production. The impacts of 10-year cropping systems (wheat-cabbage sequential cropping, wheat-corn intercrop, wheat-sunflower rotation, wheat-soybean rotation) on soil enzyme properties of surface-soil (0&ndash;20 cm) were studied. Total carbon, nitrogen, phosphorus and sulfur, and nine soil hydrolases related to nutrient availabilities (&beta;-galactosidase, &alpha;-galactosidase, &beta;-glucosidase, &alpha;-glucosidase, urease, protease, phosphomonoesterase, phosphodiesterase, arylsulphatase) and five enzymes kinetic characters were examined. Wheat-corn intercrop systems had higher total C, total N, total P and total S concentrations than wheat-soybean and wheat-sunflower rotation systems. Most test enzyme activities (&alpha;-galactosidase, &beta;-galactosidase, &alpha;-glucosidase, &beta;-glucosidase, urease, protease, phosphomonoesterase and arylsulphatase) showed the highest activities under wheat-corn intercropping system. Urease, protease and phosphodiesterase activities of wheat-cabbage sequential cropping system were significantly higher than two rotation systems. The maximum reaction rates of enzymes (V<sub>max</sub>) were higher than apparent enzyme activity, which suggests larger potential activity of enzymes, while not all kinetic parameters were adaptive as soil quality indicators in dry hilly cinnamon soil.

scholarly journals Subcellular distribution of glycosidases in human polymorphonuclear leucocytes

1978 ◽  
Vol 174 (1) ◽  
pp. 53-59 ◽  
Author(s):  
R F Rest ◽  
M H Cooney ◽  
J K Spitznagel
Keyword(s):  
Subcellular Distribution ◽  
Polymorphonuclear Leucocytes ◽  
Density Gradients ◽  
Glucosidase Activity ◽  
Mitochondrial Fractions ◽  
Specific Granules ◽  
Azurophil Granule ◽  
Alpha Galactosidase ◽  
Beta Glucosidase ◽  
Alpha Glucosidase

The subcellular distribution of nine glycosidases were studied in fractions of homogenized human polymorphonuclear leucocytes (neutrophils) obtained by isopycnic centrifugation through linear sucrose density gradients. The substrates were 4-methylumbelliferyl glycosides. All nine glycosides were hydrolysed by enzymes in neutrophil cytosol fractions, and by enzymes in at least one granule population. alpha-Glucosidase activity sedimented in sucrose density gradients to a point (p = 1.180 g/ml) just above the specific granules, possibly the ‘tertiary’ granule population. The peak corresponding to alpha-glucosidase did not co-sediment with, but considerably overlapped, the peak corresponding to lactoferrin, a marker for specific granules (p = 1.187 g/ml). alpha-Galactosidase activity was found primarily in heavy azurophil granules (p = 1.222 g/ml). alpha-Mannosidase activity was found primarily in light azurophil granules (p = 1.206 g/ml), following the distribution of myeloperoxidase, the commonly used azurophil granule marker. beta-Glucosidase activity was concentrated in mitochondrial fractions (p = 1.160 g/ml). All other glycosidases presented complex distributions, with activities not restricted to one granule class. Granule-associated glycosidase activities were increased 2–38 times when measured in the presence of 0.05% Triton X-100, indicating latency of the enzymes within granules.

scholarly journals Purification and properties of a stable β-glucosidase from an extremely thermophilic anaerobic bacterium

1987 ◽  
Vol 243 (3) ◽  
pp. 779-787 ◽  
Author(s):  
M L Patchett ◽  
R M Daniel ◽  
H W Morgan
Keyword(s):  
Anaerobic Bacterium ◽  
Thermal Inactivation ◽  
First Order ◽  
First Order Kinetics ◽  
Purification And Properties ◽  
Wide Range ◽  
Optimum Ph ◽  
Exclusion Chromatography ◽  
Beta Glucosidase ◽  
Beta Galactosidase

A beta-glucosidase (EC 3.2.1.21) was purified to homogeneity from cell-free extracts of an extremely thermophilic anaerobic bacterium. The enzyme has an Mr of 43,000 as determined by molecular-exclusion chromatography, has a pI of 4.55 and shows optimum activity at pH 6.2. The enzyme is active against a wide range of aryl beta-glycosides and beta-linked disaccharides, with beta-galactosidase activity only slightly less than beta-glucosidase activity, and significant beta-xylosidase activity. Lineweaver-Burk plots for p-nitrophenyl beta-glucoside, o-nitrophenyl beta-glucoside and cellobiose substrates are biphasic concave-downwards. Inhibition of the beta-glucosidase by substrates and glucose is negligible. Thermal inactivation follows first-order kinetics, with t1/2 (65 degrees C) 45 h, t1/2 (75 degrees C) 47 min and t1/2 (85 degrees C) 1.4 min and a deactivation energy of 380 kJ/mol at pH 6.2. At pH 7.0, which is the optimum pH for thermostability, t1/2 (75 degrees C) is 130 min. At 75 degrees C, at pH 6.2, the thermostability is enhanced about 8-fold by 10% (w/v) glycerol, about 6-fold by 0.2 M-cellobiose and about 3-fold by 5 mM-dithiothreitol and 5 mM-2-mercaptoethanol.

scholarly journals Absence of step changes in activity of certain enzymes during the cell cycle of budding and fission yeasts in synchronous cultures

1983 ◽  
Vol 61 (1) ◽  
pp. 339-349
Author(s):  
J. Creanor ◽  
S.G. Elliott ◽  
Y.C. Bisset ◽  
J.M. Mitchison
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Acid Phosphatase ◽  
Kluyveromyces Lactis ◽  
The Other ◽  
Linear Pattern ◽  
Synchronous Cultures ◽  
Asynchronous Control ◽  
Alpha Glucosidase ◽  
Beta Galactosidase

Synchronous cultures prepared by selection from an elutriating rotor were used to measure activity changes during the cell cycle of the following enzymes: acid phosphatase in Schizosaccharomyces pombe and Saccharomyces cerevisiae, alpha-glucosidase in S. cerevisiae and beta-galactosidase in Kluyveromyces lactis. There was no sign of step rises in activity in acid phosphatase but there were indications in S. cerevisiae of the linear pattern with rate doublings once per cycle that had been found previously in S. pombe. There was also no sign of step rises in the other two enzymes, in contrast to earlier results using different techniques. Asynchronous control cultures showed little or no perturbations after the first hour.

scholarly journals Hydrolysis of dietary flavonoid glycosides by strains of intestinal Bacteroides from humans

1987 ◽  
Vol 248 (3) ◽  
pp. 953-956 ◽  
Author(s):  
V D Bokkenheuser ◽  
C H Shackleton ◽  
J Winter
Keyword(s):  
Healthy Subjects ◽  
Enzymic Activity ◽  
Flavonoid Glycosides ◽  
Faecal Flora ◽  
A Cell ◽  
Bacteroides Ovatus ◽  
Dietary Flavonoid ◽  
Beta Glucosidase ◽  
Hydrolysis Of ◽  
Beta Galactosidase

Rutin and quercitrin are hydrolysed to quercetin, and robinin is hydrolysed to kaempferol, by faecal flora from healthy subjects. The enzymes required for these hydrolyses, namely alpha-rhamnosidase and beta-galactosidase, were produced by some strains of Bacteroides distasonis; other strains, however, synthesized beta-glucosidase. The last-named enzyme was also elaborated by Bacteroides uniformis and Bacteroides ovatus. All the enzymes were produced constitutively. A cell-free extract of B. distasonis containing beta-glucosidase displayed an enzymic activity of 1 mumol/10 min per 10 mg of protein.

scholarly journals The effect of low temperatures on enzyme activity

1995 ◽  
Vol 305 (1) ◽  
pp. 17-20 ◽  
Author(s):  
N More ◽  
R M Daniel ◽  
H H Petach
Keyword(s):  
Escherichia Coli ◽  
Enzyme Activity ◽  
Glutamate Dehydrogenase ◽  
Low Temperatures ◽  
Sharp Decrease ◽  
Bovine Liver ◽  
Extreme Thermophiles ◽  
Beta Glucosidase ◽  
The Stability ◽  
Beta Galactosidase

The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain AN1 and beta-glucosidase from Caldocellum saccharolyticum expressed in Escherichia coli) has been exploited to allow measurement of activity over a 175 degrees C temperature range, from +90 degrees C to -85 degrees C for the glutamate dehydrogenase and from +90 degrees C to -70 degrees C for the beta-glucosidase. The Arrhenius plots of these enzymes, and those for two mesophilic enzymes (glutamate dehydrogenase from bovine liver and beta-galactosidase from Escherichia coli), exhibit no downward deflection corresponding to the glass transition, found by biophysical measurements of several non-enzymic mesophilic proteins at about -65 degrees C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases.

Enzymic hydrolysis of sphingolipids. Hydrolysis of ceramide lactoside by an enzyme from rat brain

1966 ◽  
Vol 101 (3) ◽  
pp. 680-686 ◽  
Author(s):  
G Shimon ◽  
MR Maurice
Keyword(s):  
Fatty Acid ◽  
Rat Brain ◽  
Enzymic Hydrolysis ◽  
Beta Glucosidase ◽  
Hydrolysis Of ◽  
Beta Galactosidase

Ceramide lactoside [1-O-(galactosido-4-beta-glucosido)-2-N-acyl-sphingosine] was hydrolysed to ceramide glucoside and galactose by beta-galactosidase of rat brain. The reaction was not reversible, required cholate or taurocholate, had optimum pH5.0 and K(m) 2.2x10(-5)m. It was inhibited by gamma-galactonolactone and galactose as well as by ceramide, sphingosine and fatty acid. Ceramide lactoside could be degraded to ceramide, galactose and glucose by mixtures of rat-brain beta-galactosidase and ox-brain beta-glucosidase.

scholarly journals Effects of Various Environmental Conditions on Pulcherrimin Production and Extracellular Enzyme Profiles of Metschnikowia pulcherrima

2020 ◽  
pp. 10-16 ◽  
Author(s):  
Tülay Turgut Genç
Keyword(s):  
Heat Stress ◽  
Extracellular Enzyme ◽  
Growth Conditions ◽  
Pigment Synthesis ◽  
Yeast Strains ◽  
Metschnikowia Pulcherrima ◽  
Different Temperatures ◽  
Beta Glucosidase ◽  
Alpha Glucosidase ◽  
Leucine Arylamidase

The aim of the present study was to determine the effect of various stress conditions on pulcherrimin pigment secretion and extracellular enzyme profiles of isolated Metschnikowia pulcherrima yeast strains. In order to analyse the effects of heat stress and osmotic stress on pulcherrimin pigment synthesis, different temperatures and NaCl concentrations were used, respectively. The enzymatic profiles of M. pulcherrima yeast strains were determined by API-ZYM. The results indicated that the amount of pigment synthesis and the localization were changed depending on the growth conditions. All yeast strains showed a high leucine arylamidase, valine arylamidase, alpha-glucosidase and beta-glucosidase activities.

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