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)

B and T lymphocytes were separated by means of the spontaneous sheep red blood cell rosette formation technique from 3 normal donors. The following acid hydrolases were biochemically determined on separated B and T lymphocytes: acid phosphatase, beta-glucuronidase, beta-galactosidase, beta-hexosaminidase, alpha-arabinosidase, alpha-galactosidase, alpha-mannosidase, alpha-glucosidase, and pH 4.0 and pH 5.0 beta-glucosidase. The activities of most of the acid hydrolases including acid phosphatase and beta-glucuronidase were found to be slightly decreased in B lymphocytes when compared to T lymphocytes. However, alpha-mannosidase activity was found to be significantly higher in the B lymphocytes than in the T lymphocytes and offers the possibility of using this enzyme as a B lymphocyte marker.
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PMID:Acid hydrolases in normal B and T blood lymphocytes. 41 51

The binding of 22 human liver hydrolase activities by immobilized lectins of six different carbohydrate specificities, namely alpha-D-mannose (glucose), D-N-acetylglucosamine, D-N-acetylgalactosamine, L-fucose, alpha-D-galactose and beta-D-galactose, were examined. Differences in binding among these enzymes and within specific enzymes were observed. For example, the neutral forms of alpha-mannosidase and beta-xylosidase were bound by the Ulex europaeus lectin I (specific for L-fucose), whereas the acidic forms were not. Bandierea simplicifolia lectin (specific for alpha-galactose) bound 65% of beta-glucuronidase activity; recycling experiments demonstrated complete binding of the enzyme that had been eluted with the competitor D-galactose and no binding of the fraction that was not initially bound. These results suggested the presence of two forms of this enzyme. Similar data were obtained for acidic beta-galactosidase activity. These experiments may provide the basis for the expanded use of immobilized lectins for purification and characterization of hydrolases and other glycoproteins.
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PMID:Binding of human liver hydrolases by immobilized lectins. 42 66

It is shown that infection of chick embryo fibroblasts with agents of paratrachoma and meningopneumonia Halprowiaceae (Chlamydiaceae) causes a sharp decrease of the activities of lysosomal enzymes, e.g. acidic alpha-glucosidase, beta-glucuronidase, beta-galactosidase, alpha-mannosidase, acid phosphatase, etc. The activity of cytosol enzymes (neutral alpha-glucosidase, amylo-1,6-glucosidase) does not change, however. A decrease in the activities of lysosomal enzymes in infected fibroblasts occurs some time later after inoculation and is due to a release of lysosomal enzymes from the fibroblasts into the culture medium, without loss of cell integrity. No changes in the activity of lysosomal enzymes in fibroblasts and culture medium is observed in the case of inoculation of cells with a killed agents, as well as after contact of cells with a suspension of normal chick embryo yolk sacs. The release of lysosomal enzymes from halprowiae-infected chick embryo fibroblasts probably occurs by the exocytosis.
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PMID:[Study of lysosomal enzymes in chick embryo fibroblasts infected with microorganisms of family Halprowiaceae (Chlamydiaceae)]. 55 98

The activities of 9 acid hydrolases were determined in cell-free amniotic fluid, leucocytes and cultured fibroblasts using fluorogenic substrates. The specific activities of beta-glucosidase, alpha-fucosidase, beta-hexosaminidase, and arylsulphatase A and B were found to be in the same range in cell-free amniotic fluid and in leucocyties. The isoenzyme pattern of these 5 hydrolases as well as that of acid phosphatase and alpha-mannosidase showed some similarities in all three specimens studied; the pattern of alpha- and beta-galactosidase obtained by isoelectric focusing was different in the 2 types of cells studied and in the cell-free amniotic fluid.
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PMID:Isoelectric focusing pattern of acid hydrolases in cultured fibroblasts, leucocytes and cell-free amniotic fluid. 57 95

The pH optima and apparent Km and Vmax values were determined for nine glycosidases of the retinal pigment epithelium (RPE) of the calf. In terms of micromoles of substrate cleaved per milligram protein per hour, the following relative order of enzymatic activities was observed: beta-N-acetylglucosaminidase greater than alpha-glucosidase = beta-N-acetylgalactosaminidase greater than alpha-mannosidase greater than beta-galactosidase greater than beta-glucosidase greater than alpha-fucosidase greater than alpha-galactosidase greater than beta-glucuronidase. The pH optimum of each of these enzymes was in the acidic range (below pH 6). All these findings refer to enzymatic activities of bovine RPE preparations obtained by the brushing procedure of Glocklin and Potts and washing as described by Berman and Feeney. Thus they may relate to those activities associated with particulate components of the RPE cell and not to the more soluble glycosidases. The distribution of the glycosidases between the washes of the cells and the final pellet of bovine RPE cells was examined. The activities of 10 glycosidases in the RPE of the embryonic chick were also examined. Neither beta-mannosidase nor beta-fucosidase activities could be detected in washed bovine RPE cells, although beta-mannosidase was detected in RPE of the embryonic chick. The presence of isoenzymes of beta-glucuronidase in bovine RPE was indicated. Specificity by beta-glucuronidase of bovine RPE for synthetic substrates was observed.
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PMID:Glycosidases of the retinal pigment epithelium. 70 Sep 67

Tetrahymena were grown in proteose-peptone medium supplemented with glucose, mannose, fructose, galactose, acetate, succinate, or pyruvate and then washed and resuspended in a non-nutrient salt solution and the amounts of 7 acid hydrolases secreted into the medium in a one hour incubation were measured. Cells that had been grown in the presence of glucose secreted about half the amounts of acid phosphatase, beta-N-acetylglucosaminidase and acid protease as did control cells grown in unsupplemented medium. Pyruvate was about as effective as glucose and both were slightly more effective than acetate or fructose. Succinate had little effect. Similar experiments showed that alpha-mannosidase, beta-fucosidase, and beta-galactosidase are secreted into the salt solution and the secretion is reduced by prior growth of the cells in medium supplemented with glucose or mannose but not galactose. Except for alpha-mannosidase, these reductions in amounts of hydrolase secreted were not accompanied by appreciable changes in intracellular activity, and therefore demonstrate a persistent effect of growth in the presence of certain metabolites on the subsequent secretion of lysosomal hydrolases. Since the inhibition of subsequent secretion depended on both the individual metabolite and the particular hydrolase examined, it appears that the effect of metabolites is not limited to a general inhibition of secretion but may differentially alter some properties of lysosomal subpopulations. A preliminary characterization of the secreted acid protease of Tetrahymena suggests that there may be two acid proteases released, since up to 25% of the activity was not inhibited by high concentrations of pepstatin, leupeptin, or chymostatin.
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PMID:Effects of metabolites present during growth of Tetrahymena pyriformis on the subsequent secretion of lysosomal hydrolases. 80 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

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 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

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


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