Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Activities of three lysosomal glycosidases, beta-galactosidase, beta-glucuronidase, and N-acetyl-beta-hexosaminidase, have been shown to differ in bf/bf and bf/+ mice. Thus bf/bf mice usually have much higher activities of these enzymes in their kidney cells than bf/+ animals. There seem, however, to be some exceptions to this general pattern, especially for galactosidase of females from the C57BL/6J strain. A likely interpretation of the difference is that the bf locus has pleiotropic effects. An alternative explanation, less likely, is that a gene closely linked to bf is involved. There is also a differential response to dihydrotestosterone in different groups of mice reflected in activity changes of the three enzymes.
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PMID:Effect of a coat color locus on kidney lysosomal glycosidases in the house mouse. 84 54

Neuraminidase (EC 3.2.1.18) beta-galactosidase (EC 3.2.1.23) and beta-N-acetylglucosaminidase (EC 3.2.1.30) were studied in normal and regenerating rat liver. All these glycosidases were shown to be predominantly localized in lysosome rich fraction. The activity of lysosomal neuraminidase in regenerating rat liver increased 24 hours after partial hepatectomy, whereas those of beta-galactosidase and beta-N-acetylglucosaminidase decreased. The presence of inhibitor of neurominidase in regenerating liver homogenate was shown. Actinomycin D and cycloheximide were shown to have no significant effect on lysosomal neuraminidase in regenerating rat liver.
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PMID:[Lysosomal neuraminidase, beta-galactosidase and beta-N-acetylglucosaminidase of regenerating liver tissue]. 86 11

We recently presented data showing that mannose-6-phosphate was a potent competitive inhibitor of pinocytosis of human platelet beta-glucuronidase, and that treatment of "high-uptake" forms of the enzyme with alkaline phosphatase destroyed the high-uptake property of the enzyme without diminishing its catalytic activity. These data indicate that phosphate is a necessary component of the recognition marker on the enzyme for pinocytosis by human fibroblasts, and suggest that the phosphate on high-uptake forms of the enzyme is present as a phosphohexosyl moiety. Results presented here show that mannose-6-phosphate is also a potent inhibitor of pinocytosis of the following enzyme preparations: (a) beta-glucuronidase from human spleen, liver, placenta, and urine; (b) beta-hexosaminidase and beta-galactosidase from human platelets; (c) beta-hexosaminidase from human fibroblast secretions. Alkaline phosphatase treatment of all these enzymes except beta-galactosidase, which was unstable to the incubation conditions and could not be tested, greatly diminished the uptake activity of the enzymes without diminishing their catalytic activity. These results suggest that phosphohexosyl recognition is a general characteristic of pinocytosis of lysosomal glycosidases.
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PMID:Phosphohexosyl recognition is a general characteristic of pinocytosis of lysosomal glycosidases by human fibroblasts. 90 52

Hexosaminidase, alpha-mannosidase, beta-galactosidase, beta-glucuronidase, and arylsulphatase A were measured inperitoneal and pleural effusions from patients with benign, malignant, and inflammatory disorders. Compared with the benign transudates, all enzyme activities were moderately elevated in malignant effusions and markedly elevated in inflammatory effusions. The assay of hexosaminidase and and alpha-mannosidase indicated clearly the underlying pathology in most specimens studied. This method could be of clinical value when the cause of an effusion is in doubt, particularly since the diagnostic criteria are independent of the presence or absence of tumour cells in the aspirate.
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PMID:Diagnostic potential of lysosomal hydrolases in body cavity effusions. 93 14

Purified bovine prothrombin has been treated with different mixtures of glycosidases. Upon incubation of the prothrombin for 30 h with a combination of neuraminidase, alpha- and beta-galactosidase and beta-N-acetylglucosaminidase in 4 mM diisopropylfluorophosphate at pH 5.3 and 30 degrees C, about 70% of the carbohydrates were removed without affecting the coagulation activity. All the sialic acid and about half of the mannose, galactose and glucosamine residues were removed by this treatment.
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PMID:On the significance of the carbohydrate moieties of bovine prothrombin for clotting activity. 94 83

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

Two water-soluble complex carbohydrate storage products were isolated from tissues and urine of patients with an inherited deficiency of lysosomal alpha-L-fucosidase (fucosidosis). The major component was an oligosaccharide of approximate molecular weight 1700, indicating that it was a dekasaccharide. From a combination of sequential digestion with purified exo-glycosidases, periodate oxidation and permethylation in conjunction with gas-liquid chromatography mass spectrometric analysis, the structure was found to be: Fuc(alpha 1 leads to 2)Gal-(beta 1 leads to 4) GlcNAc (beta1 leads to 2)Man [Fuc(alpha1 leads to 2) Gal (beta1 leads to 4) GlcNAc(beta1 leads to 2) Man] (alpha 1 leads to 3/6) Man (beta1 leads to 4) GlcNAc, although there was some evidence for heterogeneity at the mannose branchpoint. This material is structurally related to the stored oligosaccharides in patients with inherited deficiencies of beta-galactosidase (G M1-gangliosidosis) and N-acetyl-beta-hexosaminidase (G M2-gangliosidosis). A dissaccharide with the probable structure Fuc(alpha1 leads to 6)GlcNAc was found in lesser amounts in tissues; both are believed to be derived from the impaired catabolism of large numbers of different glycoproteins.
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PMID:Structure of the accumulating oligosaccharide in fucosidosis. 97 44

Enzymatic activities of beta-hexosaminidase and beta-galactosidase were determined in 24 h urine specimens from patients with renal diseases, from individuals with essential hypertension and patients with other diseases. Patients suffering from various renal diseases had significantly higher activities of the beta-hexosaminidase than individuals with essential hypertension or other diseases. However for beta-galactosidase only the mean value of the enzymatic activities was elevated. The possible mechanisms causing an increase of these enzymes in 24 h urine samples are discussed.
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PMID:[Enzyme activities of beta-hexosaminidase in urine from patients with renal diseases (author's transl)]. 97 76

Approximately 70% of fucose-labeled glycopeptides from the cell surface and cellular material of rat fibroblasts (3Y1B cells) were hydrolyzed by endo-beta-N-acetylglucosaminidase D in the presence of neuraminidase, beta-galactosidase and beta-N-acetylglucosaminidase. Structure of the susceptible glycopeptides were found to be very similar to non-membrane glycopeptides of the complex heteropolysaccharide unit, such as the sialylated glycopeptides of thyroglobulin. On the other hand, the resistant glycopeptides were also refractory toward endo-beta-N-acetylglucosaminidase H and alpha-mannosidase, and appeared to be a mixture of glycopeptides with unique structures.
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PMID:Approximately 70% of fucose-labeled glycopeptides from the cell surface and cellular material of rat. 98 87

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


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