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)

beta-D-galactosidase (beta-D-galactoside galactohydrolase, E.C. 3.2.1.23) activity was localised in the digestive tract of Setaria digitata. The enzyme extract shows maximum activity in the pH range between 3.5 and 5.0 and at 45 degrees C. The enzyme shows the Km value of 3.636 mM for the substrate 6-bromo-2-naphthyl beta-D-galactoside and Vmax of 28.57 nmol 6-bromo-2-naphthol liberated mg-1 protein min-1. Activation/inhibition of the enzyme by various ions, medicinal plants and drugs has been studied. Polyacrylamide gel electrophoresis revealed that the enzyme exists as single form. The medicinal plants and the drug filarin effectively inhibit the enzyme. The significance of these results are discussed in relation to chemotherapy.
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PMID:Some properties of beta-D-galactosidase from the adult filarial nematode Setaria digitata. 211 94

Calf thymus DNA and M13mp9 RF DNA were modified with [ring-3H]2-naphthyl isocyanate (NIC) and analyzed by reverse-phase HPLC following enzymatic hydrolysis. In each case, essentially, a single radioactive component, which co-chromatographed with authentic N4-2-naphthyl-carbamoyl-2'-deoxycytidine (NCdC), was detected. In order to explore the biological potential of this adduct, mp9 RF DNA modified with NIC was introduced into Escherichia coli strains using a calcium chloride technique. The plaque-forming efficiencies of DNA decreased with increasing adduct level, and the decreases were more pronounced in Uvr endonuclease-deficient strains (i.e. AB1886, uvrA; AB1885, uvrB; AB1884, uvrC) as compared to JM103 (Uvr endonuclease proficient) and JM101 RH03 (recA). These results suggest that these lesions, NCdC adducts, can be removed by the Uvr endonuclease repair system. Mutations were detected as the loss of ability of the bacteriophage to complement the defective beta-galactosidase of the host cells. Induction of SOS functions in the host cells enhanced the mutation frequency to 0.089%, i.e. greater than or equal to 4-fold greater than in non-SOS-induced cells, in transfections with RF DNA that contained 100 adducts/molecule. The mutagenic potency of this cytidine lesion is lower than that of the guanine-C8 adducts of 2-aminofluorene and 2-acetylaminofluorene as reported previously for this mutagenesis system.
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PMID:Characterization and genotoxicity of DNA adducts caused by 2-naphthyl isocyanate. 222 33

1. The chromatography of rat small-intestinal beta-galactosidase activities on gel-filtration and ion-exchange columns has been studied. Five different substrates were used to measure beta-galactosidase activity (lactose, phenyl beta-galactoside, o-nitrophenyl beta-galactoside, p-nitrophenyl beta-galactoside and 6-bromo-2-naphthyl beta-galactoside) and the activity was measured at one acid and one more neutral pH value. 2. By gel filtration one acid beta-galactosidase, hydrolysing lactose and the hetero-beta-galactosides at about the same rate, and one more neutral beta-galactosidase, hydrolysing lactose much more rapidly than the hetero-beta-galactosides, were separated. 3. By ion-exchange chromatography the acid enzyme was fractionated into two components. These may be individual enzymes or different forms of the same enzyme.
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PMID:Rat small-intestinal beta-galactosidases. Separation by ion-exchange chromatography and gel filtration. 563 67

1. Three fractions of beta-galactosidase activity from the rat small-intestinal mucosa were separated chromatographically. Two of these fractions had an acid pH optimum at 3-4, and the third one had a more neutral pH optimum at 5.7. 2. The two ;acid' beta-galactosidase fractions had considerably lower K(m) values for hetero beta-galactosides than for lactose. The V(max.) values were similar for all the substrates used (lactose, phenyl beta-galactoside, o-nitrophenyl beta-galactoside, p-nitrophenyl beta-galactoside and 6-bromo-2-naphthyl beta-galactoside). No difference could be detected between the two ;acid' fractions with respect to their enzymic properties (pH optimum, K(m) for the different substrates, K(i) for lactose as an inhibitor of the hydrolysis of hetero beta-galactosides, K(i) for phenyl beta-galactoside as an inhibitor of the hydrolysis of lactose, and relative V(max.) for the hydrolysis of different substrates). These two fractions probably represent different forms of the same enzyme. 3. The ;neutral' fraction had similar K(m) values for all the substrates hydrolysed, but with lactose as substrate the V(max.) was much higher than with the hetero beta-galactosides. This fraction did not split phenyl beta-galactoside or 6-bromo-2-naphthyl beta-galactoside at a measurable rate. 4. Lactose was a competitive inhibitor of the hetero beta-galactosidase activities of all the three fractions, and K(i) for lactose as an inhibitor in each case was the same as K(m) for the lactase activity. Phenyl beta-galactoside was a competitive inhibitor of the lactase activity of all the three fractions. These facts strongly indicate that in all the three fractions lactose is hydrolysed by the same active sites as the hetero beta-galactosides. 5. Human serum albumin stabilized the separated enzymes against inactivation by freezing and thawing.
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PMID:Rat small-intestinal beta-galactosidases. Kinetic studies with three separated fractions. 572 84

1. The influence of pH and the kind of buffer on the hydrolysis of lactose and four hetero-beta-galactosides (phenyl beta-galactoside, o-nitrophenyl beta-galactoside, p-nitrophenyl beta-galactoside and 6-bromo-2-naphthyl beta-galactoside) by homogenates of rat small-intestinal mucosa has been studied. 2. There are at least two beta-galactosidases present in the homogenates, one with optimum pH3-4 and another with optimum pH5-6. 3. The enzyme with the lower pH optimum is mainly a heterogalactosidase. It hydrolyses lactose slowly. The other enzyme is mainly a disaccharidase, since it hydrolyses lactose much more rapidly than the heterogalactosides. 4. Under the conditions used, citrate had an inhibitory effect on the 6-bromo-2-naphthyl beta-galactosidase activity at pH3-4, but did not influence the 6-bromo-2-naphthyl beta-galactosidase activity at pH5-6 or the hydrolysis of the other substrates at any pH.
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PMID:Rat small-intestinal beta-galactosidases. Influence of pH on the hydrolysis of different substrates. 603 77

A simple, sensitive and reproducible method of detection of extracellular beta-galactosidase was worked out. beta-Galactosidase secreted by the callus culture, or the roots of sprouting plants, hydrolyzes the substrate (6-bromo-2-naphthyl-beta-D-galactopyranoside) to produce beta-D-galactose and 6-bromo-2-naphthol, which after simultaneous azocoupling with hexazotized p-rosaniline, or basic fuchsine, produce a reddish brown compound, nearly insoluble in water (a diazonium salt). The colouring under the callus culture and around it, as well as the colouring of the roots of the sprouting plants, is a manifestation of the activity of extracellular beta-galactosidase by the objects under study. The intensity of the colouring is a measure of their enzymatic activity. The share of intracellularly localized enzyme represents the majority and the share of extracellular beta-galactosidase the minority.
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PMID:[Detection of secretion of beta-galactosidase by plant cells]. 1095 59

A recombinant Rhizobium meliloti beta-galactosidase was purified to homogeneity from an Escherichia coli expression system. The gene for the enzyme was cloned into a pKK223-3 plasmid which was then used to transform E. coli JM109 cells. The enzyme was purified 35-fold with a yield of 34% by a combination of DEAE-cellulose (pH 8.0) and two sequential Mono Q steps (at pH 8.0 and 6.0, respectively). The purified enzyme had an apparent molecular mass of 174 kDa and a subunit molecular weight of 88 kDa, indicating that it is a dimer. It was active with both synthetic substrates p-nitrophenyl beta-D-galactopyranoside (PNPG) and o-nitrophenyl beta-D-galactopyranoside (ONPG) with K(m)(PNPG) and K(m)(ONPG) of 1 mM at 25 degrees C. The k(cat)/K(m) ratios for both substrates were approximately 70 mM(-1) sec(-1), indicating no clear preference for either PNPG or ONPG, unlike E. coli beta-galactosidase. After non-denaturing electrophoresis, active beta-galactosidase bands were identified using 5-bromo-4-chloro-3-indolyl beta-D-galactopyranoside (X-gal) or 6-bromo-2-naphthyl beta-D-galactopyranoside (BNG) and diazo blue B.
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PMID:Purification and some characteristics of a recombinant dimeric rhizobium meliloti beta-galactosidase expressed in escherichia coli. 1133 53

A simple, rapid and reproducible procedure for the identification of extracellular Californian poppy (Eschscholzia californica Cham.) beta-galactosidase is described using callus cultures of seedlings from the tested plant, roots of 4-days-old seedlings of Californian poppy germinating on agar plates and cell suspension cultures cultivated from callus cultures. 6-Bromo-2-naphthyl-beta-D-galactopyranoside and p-nitrophenyl-beta-D-galactopyranoside were used as substrates for the determination of the intracellular and extracellular activities of beta-galactosidase. The extracellular beta-galactosidase activity was identified by evaluating the dye-zones in an agar medium. The enzyme from Californian poppy callus cultures or from seedling roots cultivated on agar plates supplemented with 6-bromo-2-naphthyl-galactopyranoside hydrolyzed this substrate releasing 6-bromo-2-naphthol. By simultaneous coupling with hexazonium p-rosaniline the corresponding (reddish-brown) azo-dye was formed. The agar plate method described permits rapid, simple and specific detection of plant producers of extracellular beta-galactosidase.
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PMID:A simple method for the identification and assay of extracellular plant beta-galactosidase. 1193 45

Chloroplasts prepared from mesophyll protoplasts of the primary leaf of wheat (Triticum aestivum L. cv Egret) contain about 50% of the cellular beta-galactosidase (EC 3.2.1.23) activity. More than 80% of this activity is associated with the stroma and most of the remainder, although tightly bound to the thylakoids, can be washed free with sodium pyrophosphate. The vacuole contained about 20% and the remaining enzyme was presumed to be cytoplasmic or associated with one of the other organelles. Both the vacuolar and chloroplast enzymes were capable of releasing galactose from the galactolipid monogalactosyldiacylglycerol. Apart from their distinct locations within the cells, we conclude that the enzymes are different because they differed with respect to assay pH-optimum, comparative activity against the synthetic substrates phenyl-beta-d-galactoside, 4-methylumbelliferyl-beta-d-galactoside, 6-bromo-2-naphthyl-beta-d-galactoside, the disaccharide lactose, and the inhibitors d-galactose and d-galactono-1,4-lactone.
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PMID:Characteristics of a beta-Galactosidase Associated with the Stroma of Chloroplasts Prepared from Mesophyll Protoplasts of the Primary Leaf of Wheat. 1666 31