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)

The activities of acid phosphatase, beta-glucuronidase, beta-galactosidase, acid ribonuclease, and acid deoxyribonuclease were studied in the blood serum of rats after total, either single or franctionated, exposure. After the single, total exposure to 800 R of X-rays, remarkable increases in the activities of acid phosphatase and acid deoxyribonuclease were observed in the blood serum immediately after the irradiation. At later stages were observed statistically significant decreases of beta-glucuronidase and beta-galactosidase in the rat blood serum after the total, single exposure. The serum acid ribonuclease activity remained essentially unaltered over the whole time interval of interest. In the blood serum of the rats exposed to total, fractionated irradiation, statistically significant decreases in the acid phosphatase and beta-glucuronidase activities were observed 1 and 8 days after completing the irradiation. In the case of beta-galactosidase, this decrease lasted even up to the 15th day after the end of irradiation. The activities of serum acid deoxyribonuclease and acid ribonuclease exhibited no statistically significant changes.
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PMID:Changes of the activity of certain lysosomal enzymes in the blood serum of whole-body irradiated rats. 89 16

Despite the rapidly expanding clinical use of leukocyte biochemistry, there is a limited amount of data available on normal human leukocytes. Some of the problems associated with the clinical use of leukocytes are discussed briefly. Enzyme activities of alkaline and acid phosphatase, lysozyme, and beta-galactosidase are presented. Results are reproducible between normals when expressed per mg of leukocyte deoxyribonucleic acid (DNA). Much higher lymphocyte activties of lysozyme and alkaline phosphatase are noted than previously reported with cytochemical or intact cell systems. It has been demonstrated that leukocytes cannot be considered chemically homogenous but should be separated and considered as individual cell types.
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PMID:Repetitive tissue biopsy by venipuncture: enzyme activities in isolated leukocyte populations. 94 81

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

In seven patients with cerebral atrophy due to pre-senile dementia and/or cerebrovascular disease, the activity of acid phosphatase in lumbar cerebrospinal fluid (CSF) was higher (p less than 0.05) than in six controls. The activity of arylsulphatase and beta-galactosidase in CSF was the same in the two groups. In the serum, the activities of acid phosphatase and arylsulphatase were the same in the two groups but the activity of beta-galactosidase was lower (p less than 0.02) in patients with cerebral atrophy.
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PMID:Lysosomal enzymes in cerebral atrophy. 96 91

Gel-forming mucosal glycoproteins strongly interfere with standard methods of cell fractionation. Thus, acid hydrolase-bound particles imbedded in the gel, sediment on centrifugation, in the nuclear fraction of homogenates of canine antral mucosa. These particles can be cleared by direct solubilization of the gel; however, the viscosity of the solution obtained prevents sedimentation of some of the latent hydrolases, even at very high speeds. The use of a new step-wise scheme of centrifugation and dilution successfully isolates lysosomal particles containing acid hydrolases from mucin-rich mucosa. All of the enzymes investigated, including acid phosphatase, cathepsin D, alpha- and beta-galactosidase, beta-B-acetylhexosaminidases, but with the exception of alpha-fucosidase, were found to be particle bound, exhibiting high degrees of latency. However, active mucosal particles are polydisperase in size and density, sedimenting under different centrifugal forces.
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PMID:Establishment of the integrity of lysosomes in a glycoprotein-rich matrix. Distribution pattern of seven lysosomal enzymes in gastric mucosa. 97 20

The distribution of acid phosphatase, beta-N-acetylglucosaminidase, beta-glucuronidase, and acid beta-galactosidase was studied in mm. extensor digitorum longus, soleus, and diaphragm of rats. Using the technic of semipermeable membranes activities of these enzymes were demonstrated beside cells of the interstitial tissue in muscle fibers themselves as well. Acid phosphatase displayed the highest activity which appeared in many small dots dispersed in the fiber. The activity of acid phosphatase was about 1.2 X higher in the m. soleus than in the m. extensor digitorum longus. In the latter muscle a somewhat higher activity was often found in muscle fibers displaying a higher staining for NADH tetrazolium reductase. The activity of beta-N-acetylglucosaminidase was slightly lower, that of beta-glucuronidase very weak but still discernible. The activity of acid beta-galactosidase was not ascertained in the majority of fibers. The ratio of activities measured in an area of the same size in cells of the interstitial tissue and in muscle fibers amounted in average to 2.6:1 in the case of acid phosphatase, 2.5:1 in the case of beta-N-acetylglucosaminidase, 5.7:1 in the case of beta-glucuronidase, and 44.3:1 in the case of acid beta-galactosidase. The importance of the histochemical technic in studies concerned with acid hydrolases in striated muscle fibers in normal and pathological conditions is pointed out.
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PMID:Histochemistry of some acid hydrolases in striated muscles of the rat. 99 74

Parenchymal and nonparenchymal cells were isolated from the livers of female BN/BiRij rats, aged 3, 12, 24 and 30-35 months, by means of enzymatic techniques. About 70% of the cells in the nonparenchymal cell suspensions were endothelial cells and 25% were Kupffer cells. More than 90% of the isolated parenchymal, Kupffer and endothelial cells were viable as judged by trypan blue exclusion and ultrastructural appearance. The age-related changes in the specific activities of the lysosomal enzymes acid phosphatase, beta-galactosidase, cathepsin D and arylsulphatase B in parenchymal and nonparenchymal cells showed no correlated behavior. The most prominent change was observed for the cathepsin D activity in parenchymal cells, which nearly triples during the lifespan of the rat. A comparison of the activities obtained with homogenates of the whole liver and with parenchymal and nonparenchymal cells revealed that aging changes in lysosomal enzyme activities in homogenates should be carefully interpreted, since opposite patterns of change were often observed in the activities in parenchymal cells and in nonparenchymal cells.
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PMID:Lysosomal enzyme activities in parenchymal and nonparenchymal liver cells isolated from young, adult and old rats. 99 58

1. Structure-linked latency, a trait for most lysosome hydrolase activities, is customarily ascribed to the permeability-barrier function performed by the particle-limiting membrane, which shields enzyme sites from externally added substrates. 2. The influence of various substrate concentrations on the reaction rate has been measured for both free (non-latent) and total (completely unmasked by Triton X-100) hydrolase activities in rat liver cell-free preparations. The substrates were: beta-glycerophosphate, phenolphthalein mono-beta-glucuronide. p-nitrophenyl N-acetyl-beta-D-glucosaminide and p-nitrophenyl beta-D-galactopyranoside. The ratio (free activity/total activity) X 100 is called fractional free activity at any given substrate concentration. 3. The fractional free activity of beta-glucuronidase and beta-N-acetylglucosaminidase were clearly independent of substrate concentration, over the range examined, in both homogenates and lysosome-rich fractions. The fractional free activity of acid phosphatase appeared to be either unaffected (homogenate) or even depressed (lysosome-rich fraction) by increasing the beta-glycerophosphate concentration. The fractional free activity of beta-galactosidase consistently showed a non-linear increase with increasing substrate concentration in both homogenates and lysosome-rich fractions. 4. Procedures such as treatment with digitonin, hypo-osmotic shock and acid autolysis, although effective in causing varying degrees of resolution of the latency of lysosome hydrolase activities, were unable to modify appreciably the pattern of dependence or independence of their fractional free activities on substrate concentration, as compared with that exhibited by control preparations. Ouabain did not affect the free beta-N-acetylglucosaminidase activity of liver homogenates at all. 5. Preincubation of control preparations with beta-glycerophosphate or p-nitrophenyl beta-galactoside did not result in any significant stimulation of the free hydrolytic activity toward these substrates. 6. The results consistently support the view that the membrane of "intact" lysosomes is virtually impermeable to all the substrates tested, except for p-nitrophenyl beta-galactoside, for which the evidence is contradictory. Moreover the progressive unmasking of the hydrolase activities produced by these procedures in vitro reflects the increasing proportion of enzyme sites that are fully accessible to their substrates rather than a graded increase in the permeability of the lysosomal membrane.
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PMID:Structural equivalents of latency for lysosome hydrolases. 104 Dec 36

The levels of four acid hydrolases, beta-N-acetyl glucosaminidase, beta-glucuronidase, beta-galactosidase, and acid phosphatase, and the extent of their release (release II) by thrombin was determined in platelets from nine normal subjects, nine patients with storage pool disease, and in normal platelets which had been exposed to aspirin. The levels of all four hydrolases were normal in patients with SPD. However, release of three of these hydrolases (acid phosphatase was an exception) by low concentrations of thrombin (0.015 and 0.04 U/ml) was decreased in the patients as a group, although considerable variation in the extent of release of each enzyme was noted. In contrast, aspirin failed to inhibit release II in normal platelets (except for a slight impairment in the release of beta-N-acetyl glucosaminidase), although release I (serotonin, ATP and ADP) was inhibited. All release defects could be overcome by using higher concentrations of thrombin (0.2 U/ml). The normal levels of acid hydrolases in the platelets of patients with SPD (who are deficient in the platelet dense granules) suggest that these enzymes are not normally stored in the dense granules, but rather in alpha-granules. The findings also support the conclusions of previous studies that the release reaction is impaired in SPD. This release defect appears to be different from that seen in normal platelets after exposure to aspirin.
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PMID:Content and thrombin-induced release of acid hydrolases in gel-filtered platelets from patients with storage pool disease. 113 24

Cationic proteins of brain lysosomes (LCP), myelin (MCP) and nuclear histone fractions from calf thymus (T) and rat brain (B) are shown to increase at different degree the permeability of brain lysosomes and neutrophiles for acid RNAase, acid phosphatase, catepsin D and beta-galactosidase. According to the effectivity, basic proteins can be listed in the following order: for lysosomes-f2aT, F3B, f3T greater than total histones B, f2bT greater than f2B greater than LCP, MCP greater than flT, flB; for neutriphiles-f3T larger than or equal to total histones B larger than or equal to f3b MCP larger than or equal to f2aT, f2bT greater than f2B greater than LCP greater than flB greater than flT. Fractions f2a and f3 considerably increased the release of acid RNAase from lysosomes in very low concentrations beginning from 0,2 mug/ml, while the release of catepsine and acid phosphatase took place beginning from 5-10 mug/ml. The effect of lysosome and myelin cationic proteins on the release of hydrolases occurred at concentrations ten to hundred times higher.
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PMID:[Effect of brain and thymus cationic proteins on membrane permeability]. 120 52


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