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)

Optimal assay conditions are described for 8 hydrolases of Euglena gracilis var. bacillaris, SM-L1 (streptomycin-bleached) strain, 7 of which have an acid pH-optimum. Acid-phosphatase, beta-galactosidase, beta-glucosidase, b-fucosidase, cathepsin D, RNase, DNase, and an esterase are active in cell homogenates. Amylase has very low activity, and beta-glucuronidase, arylsulfatase, beta, N-acetyl-glucosaminidase, alpha-fucosidase, and alpha- and beta-mannosidase are inactive.
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PMID:Hydrolytic enzymes of Euglena gracilis: characterization and activity as a function of culture age and carbon deprivation. 0 4

The optimal reaction conditions and kinetic properties of eleven leukocyte acid hydrolases determined with the use of fluorigenic derivatives of 4-methyl-umbelliferone are described. The enzymes studied were acid phosphatase, aryl sulfatase, alpha- and beta-glucosidase, alpha- and beta-galactosidase, alpha-mannosidase, N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucuronidase and alpha-fucosidase. More than 90% of the activity of each enzyme was released into a 27,000 X g supernatant by a double sonication procedure employing 0.9% sodium chloride and 0.1% Triton X-100. The Km values obtained were similar to those previously reported for chromogenic subtrates. A single Km value could not be derived for beta-galactosidase because its double reciprocal plot was not linear. All enzymes could be measured with less than 10 mug of protein within 15 min. Activators and inhibitors studied included the chloride salts of Na+, K+, Zn2+, Ca2+, Mg2+, Hg2+, and Fe2+ as well as p-chloromercuriphenysulfonate, glutathione, BAL, EDTA, EGTA, Triton X-100 and sodium taurocholate. The reaction conditions described in this report can be used for the diagnosis of various lysosomal storage diseases and should facilitate the development of automated procedures for the analysis of these eleven enzyme activities with small quantities of blood.
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PMID:Human leukocyte acid hydrolases: characterization of eleven lysosomal enzymes and study of reaction conditions for their automated analysis. 0 26

Changes of activity of several glycosidases (beta-galactosidase, beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, alpha-D-mannosidase and alpha-L-fucosidase) were compared in the forebrain and cerebellum during postnatal development of the rat. Detailed analysis of the data showed similarities, but also substantial differences in their development in both organs. This is interpreted as an indication of the presence of common regulatory mechanisms, as well as of other factors which differently influence development of the glycosidases studied in both CNS parts.
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PMID:Comparison of postnatal development of several acid glycosidases in the rat forebrain and cerebellum. 2 Jan 69

Assay of alpha-L-iduronidase, heparin sulphamidase, N-acetyl-alpha-D-glucosaminidase, arylsulphatase B, alpha-L-fucosidase, beta-glucuronidase, beta-galactosidase and alpha-D-mannosidase in cultured cells is described. Activities in deficient fibroblast strains are compared to control fibroblast strains. The first case of Sanfilippo B in the United Kingdom is reported. A comparison of enzyme activities in cultured fibroblasts and amniotic fluid cells is made.
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PMID:Diagnosis of the mucopolysaccharidoses using cultured skin fibroblasts and amniotic fluid cells. 11 32

1. The elution profiles of eleven acid hydrolases from human liver and plasma were directly compared using a system whereby a single salt gradient was simultaneously applied to two DEAE-cellulose chromatographic columns. 2. Plasma alpha-L-fucosidase, alpha-mannosidase, alpha-galactosidase and alpha-glucosidase isoenzymes were eluted at higher salt concentrations than the corresponding liver isoenzymes whereasbeta-N-acetylglucosaminidase, beta-galactosidase, beta-glucosidase, exo-1,4-beta-xylosidase and alpha-L-arabinofuranosidase isoenzymes were eluted at lower salt concentrations. The elution profiles of beta-glucuronidase and acid phosphatase weremore complex. 3. After incubation with neuraminidase most plasma hydrolases were eluted at lower salt concentrations, however the elution patterns of beta-glucosidase, beta-xylosidase and acid phosphatase were not altered. 4. Preincubation with neuraminidase had no effect on the elution profiles of six liver hydrolases whereas the major isoenzymes of alpha-mannosidase, beta-galactosidase and alpha-L-arabinofuranosidase were eluted at markedly lower salt concentrations. Liver alpha-fucosidase and alpha-galactosidase were eluted at slightly lower salt concentrations afterincubation with neuraminidase. 5. The results are discussed in relation to thepathogenesis of Mucolipidosis II (I-cell disease), and the synthesis and packaging of lysosomal enzymes.
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PMID:Effect of neuraminidase on the chromatographic behaviour of eleven acid hydrolases from human liver and plasma. 19 Dec 58

This is a review of the properties and molecular genetics of six lysosomal hydrolases: beta-galactosidase, hexosaminidases A and B, alpha-galactosidase, beta-glucosidase and alpha-fucosidase. Each enzyme is discussed with regards to isoenzymes and substrate specificity, subunit structure, genetic relationship of isoenzymes and genetic variants. The molecular genetics of human diseases caused by deficiencies of each enzyme are discussed.
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PMID:Glycosphingolipid hydrolases: properties and molecular genetics. 20 Aug 37

The activities of 6 glycosidases (n-acetyl-beta-glucosaminidase, beta-galactosidase, beta-glucuronidase, alpha-galactosidase, alpha-fucosidase and alpha-mannosidase) in the oviduct of the quail (Coturnix coturnix japonica) were studied with histochemical methods. Alpha-galactosidase and alpha-fucosidase showed a weak to moderate activity in the surface epithelium and in most of the glands of the oviduct. A Distinct reactivity of beta-glucuronidase was observed in the surface epithelium of the whole oviduct and in the glands of the uterovaginal-region. A moderate to distinct reactivity of n-acetyl-beta-glucosaminidase cound be demonstrated in the epithelium and in the glands of all regions of the oviduct. The comparatively highest activity of this enzyme was found in the glands of the magnum and in the surface epithelium of the uterus. The possible functions of the glycosidases in the oviduct are discussed briefly.
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PMID:[Histotopic of glycosidases in the oviduct of the quail (Coturnix coturnix japonica) (author's transl)]. 20 47

The histochemical distribution of six glycosidases (N-acetyl-beta-glucosaminidase, beta-galactosidase, beta-glucuronidase, alpha-galactosidase, alpha-mannosidase and alpha-fucosidase) was investigated in the prostate, glandula vesicularis and glandula bulbourethralis of castrated and non-castrated adult boars. The functions of the glycosidases in the male accessory sex glands of the boar and their androgen dependence are discussed briefly.
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PMID:[Histotopography of glycosidases in the accessory glands of the boar before and after castration]. 20 54

K-m values of beta-N-acetylglucosaminidase (2-acetamido-2-deoxy-beta-D-glucoside acetamidodeoxyglucohydrolase EC 3.2.1.30), beta-N-acetylgalactosaminidase (EC 3.2.1.53), beta-galactosidase (beta-D-galactoside galactohydrolase EC 3.2.1.23) and alpha-L-fucosidase (alpha-L-fucoside fucohydrolase EC 3.2.1.51) of distal colonic tumours, induced in rats by 1,2-dimethylhydrazine, were found to be significantly different compared with the values for the enzymes of the colonic mucosa of the control and tumour-bearing animals and of the proximal colonic tumours. The inhibition kinetics data also showed a significant difference between the enzymes of the distal colon tumours and of other experimental tissues. The data on the effect of pH on enzyme kinetics (pK values) showed no significant difference in the catalytic groups of the active centres of enzymes from tumours and from the control colonic mucosa. Tumour beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase compared with the enzymes from other experimental tissues were found to be different in their thermal inactivation kinetics. K-m values of 14 days old foetal intestinal beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase were significantly different from the values obtained for the adult mucosal enzymes but were similar to those of the distal colonic tumour enzymes.
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PMID:Studies on the kinetics of glycosidases from chemically-induced rat colonic tumours and normal rat colon. 23 55

Biochemical studies are presented on two siblings with some features of Mucolipidosis III, but with distinctive clinical findings. Levels of beta-galatosidase, alpha-mannosidase, beta-glucuronidase, N-acetyl-beta-glucosaminidase and alpha-fucosidase found in serum from these patients ranged from 10 to 10 times higher than normal. The ratio of heat stable to heat labile serum isoenzymes of N-acetyl-beta-glucosaminidase is considerably greater than normal. An extremely low activity of beta-galactosidase was found in fibroblasts cultured from one patient. Levels of the remaining enzymes were in the low normal range. Similarly, beta-galactosidase levels were low in heart, kidney, liver, spleen and lung of one patient who died during the course of the study. Activities of the remaining enzymes were close to normal. No excessive excretion of mucopolysaccharide was noted, however, changes in distribution of several fractions were found. Mucopolysaccharide labeled with radioactive sulfate was degraded by cultured fibroblasts at a normal rate. In addition to clinical differences, the biochemical studies further demonstrate the uniqueness of these patients.
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PMID:A new variant mucolipidosis: biochemical investigations on two siblings. 41 May 66


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