Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.23 (beta-galactosidase)
14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Various fractions obtained from normal human liver homogenates by gel chromatography and selective adsorption and elution from insolubilized concanavalin A were compared as to their beta-galactosidase and beta-glucosidase activities. The high-molecular-weight acidic beta-galactosidase form was converted into the smaller major form by sodium dodecyl sulfate treatment. Electrophoresis and electrofocusing on acrylamide slabs revealed, in addition to the two major isoenzyme forms (acid and neutral), another five minor bands with enzymatic activity.
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PMID:Separation of beta-galactosidases and beta-glucosidases from human liver. 93 25

The effect of Fusarium sporotrichiella v. sporotrichioides mycotoxin (sporofusarin) on the total and non-sedimentary supernatant activity of 13 marker-enzymes of subcellular particles (2 mitochondrial enzymes-cytochrome oxidase and malate dehydrogenase; 8 lysosomal enzymes -- acid phosphatase, acid RNAase, acid DNAase, arylsulphatases A and B, beta-N-acetylglucosaminidase, beta-glucuronidase, beta-galactosidase and beta-glucosidase; 2 microsomal enzymes -- glucose-6-phosphatase and acetylesterase; plasma membrane enzyme -- alkaline phosphatase) of the rat liver, kidney, spleen and bone-marrow was studied in in vivo experiments. The latter demonstrated that sporofusarin effects were characterized by a significant organ and organella specificity, viz. the toxin caused a sharply increased activity, mainly of lysosomes enzymes and labilization of the lysosomal membranes, primarily in the spleen and the bone-marrow. A conclusion is drawn that the discovered selective destructive action of sporofusarin on the lysosomes may be regarded as a new phenomenon that, possibly is directly related to the characterization of the mechanism responsible for a specific effect produced by sporofusarin.
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PMID:[Lysosomal component in the mechanism of the toxic effect of sporofusarin]. 94 27

A number of adsorbents useful for purifying glycosidases were synthesized and their adsorption and characteristics were examined using partially purified glycosidase mixtures from Takadiastase or soybean. These adsorbents were prepared by coupling di-epsilon-aminocaproyl-p-aminophenyl N-acetyl-1-thio-beta-D-glucosaminide, beta-D-glucoside, beta-D-galactoside or alpha-D-mannoside with CNBr-activated Sepharose 4B. Many glycosidases were adsorbed on the four adsorbents at low ionic strength, and increase of the ionic strength caused the enzymes to be eluted. However, the specificity of the adsorbents, contrary to our expection, was very low. All of these adsorbents adsorbed Taka N-acetyl-beta-D-glucosaminidase [EC 3.2.1.30], Taka beta-D-glucosidase [EC 3.2.1.21], and Taka beta-D-galactosidase [EC 3.2.1.23] at low ionic strength. The order of elution of these three enzymes by a linear gradient of ionic strength was the same in the four adsorbents, the order being beta-D-galactosidase, beta-D-glucosidase, and N-acetyl-beta-D-glucosaminidase. Soybean glycosidases also showed nearly the same elution pattern, though the ionic strength of the eluate was slightly lower than with Taka glycosidases. Soybean alpha-D-mannosidase [EC 3.2.1.24] was also adsorbed on these adsorbents, and was eluted between beta-D-glucosidase and N-acetyl-beta-D-glucosaminidase. These adsorption phenomena were not specific as regards the structure of the glycoside moiety, but they were useful for purifying glycosidases, possessing good reproducibility with easy activation and mild operating conditions.
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PMID:Affinity chromatography of glycosidases. Preparation and properties of affinity column adsorbents. 94 2

The latency of the alpha-glucosidase activity of intact rat liver lysosomes was studied by using four substrates (glycogen, maltose, p-nitrophenyl, alpha-glucoside, alpha-fluoroglucoside) at a range of substrate concentrations. The results indicate that the entire lysosome population is impermeable to glycogen and maltose, but a proportion of lysosomes are permeable to alpha-fluoroglucoside and a still higher proportion permeable to p-nitrophenyl alpha-glucoside. Incubation at 37 degrees C in an osmotically protected buffer of of pH 5.0 caused lysosomes to become permeable to previously impermeant substrates and ultimately to release their alpha-glucosidase into the medium. The latencies of lysosomal beta-glucosidase and beta-galactosidase were examined by using p-nitrophenyl beta-glucoside and beta-galactoside as substrates. The results indicate permeability properties to these substrates similar to that to p-nitrophenyl alpha-glucoside. On incubation in an osmotically protected buffer of pH 5, lysosomes progressively released their beta-galactosidase in soluble form, but beta-glucosidase remained attached to sedimentable material. Lysosomal beta-glucosidase was inhibited by 0.1% Triton X-100; alpha-glucosidase and beta-galactosidase were not inhibited.
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PMID:Latency of some glycosidases of rat liver lysosomes. 101 43

The effect of the mycotoxin of Fusarium sporotrichiella v. sporotrichioides (sporofusarin) was studied in vitro on the total and nonsedimenting activity of eight lysosomal enzymes: acid ribonuclease, aryl sulfatases A and B, beta-glucuronidase, alpha- and beta-galactosidases, beta-glucosidase, beta-acetylglucosaminidase, and alpha-mannosidase. Incubation of a suspension of rat liver lysosomes with an aqueous solution of sporofusarin led to inhibition of the total activity of the membrane-bound lysosomal enzyme beta-glucosidase. In a dose of only 1.6 x 10-5 M sporofusarin caused a significant increase in the nonsedimenting activity of nearly all the enzymes; in a concentration of 1.6 x 10-3 M most of the enzymes of the lysosomal matrix (beta-glucuronidase, beta-galactosidase, aryl sulfatases A and B) were liberated almost completely into the supernatant, and nearly all the beta-glucosidase also was liberated. It is postulated that damage to the subcellular membranes is an important component of the toxic action of sporofusarin.
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PMID:Action of the mycotoxin of Fusarium sporotrichiella v. sporotrichioides on lysosomal membranes. 111 54

The authors present the results of study or fegularities attending the changes in the activity of free, total and bound fractions of the lysosomal enzymes--beta-glucosidase and beta-galactosidase in the thymus and the spleen of rabbits under conditions of DOCA administration. The activity of the enzymes was studied 30 min, 1, 4, 12, 24 and 48 hours after a single injection of the hormone. DOCA administration caused biphasic changes in the activity of both glycosidases. A marked increase in the activity of all the enzyme fractions during the first experimental hours was later replaced by their fall. An increase in the activity of glycosidases at the early periods of DOCA administration pointed to the intensification of the enzymatic synthesis, and also could be associated with the spicific induction of the enzymatic activity. The activity of beta-glucosidase and of beta-galactosidase directly depended on DOCA dose. Effects similar to the experiments in vivo were obtained in vitro. The activity of hyaluronidase under the effect of Dca decreased considerably in the thymus and the spleen, particularly at the early experimental periods, pointing to reduction of tissue permeability of the lymphoid organs.
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PMID:[The effect of desoxycorticosterone acetate on the activity of the lysosomal enzymes of lymphoid organs]. 113 80

KB cells were synchronized by a double thymidine block procedure. An investigation was made of the activities of alpha-L-fucosidase (EC 3.2.1.51), alpha-D-galactosidase (EC 3.2.1.22), beta-D-galactosidase (ec 3.2.1.23), alpha-D-glucosidase (EC 3.2.1.20), beta-D-glucosidase (EC 3.2.1.21), alpha-D-mannosidase (EC 3.2.1.24), beta-D-N-acetylgalactosaminidase (EC 3.2.1.53), and beta-D-N-acetylglucosaminidase (EC 3.2.1.52) from synchronized cultures, using appropriate artificial substrates. Ceramide glucosidase (EC 3.2.1.45) and ceramide trihexosidase levels (EC 3.2.1.47) were also investigated at various stages in the cell cycle, using appropriate glycosphingolipid substrates. Whereas each of these enzymes exhibited some activity throughout the cell cycle, peak activity (2- to 6-fold increase) occurred late in the S phase. Two molecular forms of ceramide glucosidase (optimal activity at pH 4.0 and pH 6.0) and two forms of ceramide trihexosidase (pH 4.0 and pH 7.5) were identified. Peak levels of the forms that preferred the relatively acid pH occurred earlier in the S phase of the cell cycle than those of the forms that were more active at the higher pH. The possibility that the forms with optimal activity at pH 4 are precursors of those with optimal activity at pH 6 to 7.5 is discussed. Precipitation of beta-galactosidase of synchronized KB cells with specific antibody revealed that changes in the activity of this enzyme during the cell cycle were the result of fluctuations in the amount of the enzyme.
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PMID:Glycosphingolipid glycosyl hydrolases and glycosidases of synchronized human KB cells. 115 Jun 49

1. The rates of accumulation (enzyme units/h per 10(8) cells) of a number of glycosidase activities were studied in Dictyostelium discoideum cells during the growth and differentiation phases of this organism's life cycle. 2. The rates of accumulation of the enzymes beta-N-acetylglucosaminidase, alpha-glucosidase and beta-galactosidase remain unchanged during the growth and early differentiation phases. 3. The considerable changes in specific activity of the enzymes which occur in the early differentiation phase are due to the massive loss of total cellular protein which occurs at this time. 4. Significant alterations can occur in the rates of accumulation of alpha-mannosidase during both the growth and differentiation phases, and since, on the onset of differentiation, beta-glucosidase activity is excreted and degraded, the rate of accumulation of this enzyme differs in the growth and differentiation phases. 5. The characteristic rates of accumulation of all these glycosidases change markedly with changes in the growth conditions of the myxamoebae, and thus these rates of synthesis must be regulated independently; however, addition of cyclic AMP to the growth medium has no effect on them.
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PMID:Rates of accumulation of glycosidase activities during growth and differentiation of Dictyostelium discoideum. 117 88

N-Acetyl-beta-glucosaminidase, beta-galactosidase, beta-glucosidase, acid and alkaline phosphatase were monitored in urine kidney homogenates and serum of rats with papillary damage induced with ethyleneimine. Serum urea levels, total protein in the urine and urine volume were monitored throughout the study. Histological studies showed that the injection of ethyleneimine caused immediate papillary necrosis, followed later by secondary cortical involvement. Minor papillary necrosis induced by a low dose (0.5 mul/kg) of ethyleneimine was characterised by a rise in urinary N-acetyl-beta-glucosaminidase activity which was followed later by an increase in the activity of the other enzymes monitored. More severe papillary necrosis induced with a higher dose of ethyleneimine (5.0 mul/kg) resulted in an immediate rise in the activities of all the urinary enzymes which then decreased only to rise again when cortical involvement occurred. Serum urea was unaltered but urine volume and protein were increased coincidentally with the urinary enzyme activities. The value of the assay of urinary enzymes in distinguishing papillary from glomerular and tubular damage is assessed. The possible relevance of the ethyleneimine model to the etiology of papillary nephropathy is discussed.
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PMID:Urinary enzyme excretion during renal papillary necrosis induced in rats with ethyleneimine. 120 12

Effect of different concentration of non-ionic detergents (Triton X-100, Triton X-305, BRIJ-35 and Triton WR-1339) on total and non-sedimentable activity of 8 rat liver lysosome enzymes (acid phosphatase, acid DNase, acid RNase, arylsulphatases A and B, beta-glucuronidase, beta-galactosidase, beta-glucosidase and beta-acetylglucosaminidase) was studied. Only Triton X-100 at the concentration of 0.1% (and higher) was found to release completely lysosome enzymes. Low concentrations of Triton X-100 (0.025-0.05%) were used to characterize the strength of enzyme binding: the level of releasing acid DNase, beta-galactosidase, beta-glucuronidase and acid phsophatase being considerably higher than that of other lysosome enzymes studied. On the basis of the data obtained a method is worked out, which is suitable for series studies of the stability of lysosome membranes under different physiological and pathological conditions. The essence of the method is the treatment of membrane particles with increasing concentrations of Triton X-100 (0.025; 0.05 AND 0.1%) AND THE SUCCESSIVE ESTIMATION OF NON-Sedimentable activity of marker enzymes. The method detected troubles in the stability of rat liver lysosome membranes under starvation, protein deficiency and aging.
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PMID:[Determination of lysosome membrane stability]. 120 72


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