Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

GM1 ganglioside beta-galactosidase (GM1-beta-galactosidase) was purified from normal cat brain and liver by a combination of classical and affinity procedures. The final preparation of brain GM1-beta-galactosidase was enriched over 2000-fold with a 36% yield. However, the product was shown to contain several components by disc gel electrophoresis. GM1-beta-galactosidase was also purified from liver with greater than a 30 000-fold enrichment and 40% yield. The liver enzyme was judged homogeneous by disc gel electrophoresis at pH 4.3, 8.1, and 8.9 and by gel chromatography. Both liver and brain GM1-beta-galactosidase(s) eluted as sharp symmetrical peaks from Sephadex G-200 with molecular weights of 250 000 +/- 50 000. The apparent Km determined for 4-methylumbelliferyl beta-D-galactopyranoside (4-MU-Gal) using partially purified brain GM1-beta-galactosidase was 1.73 X 10(-4) M. Liver GM1-beta-galactosidase gave a Km with 4-MU-Gal of 3.25 X 10(-4) M and for [3H]GM1 ganglioside a Km of 4.51 X 10(-4) M was calculated. The pH optima of brain and liver GM1-beta-galactosidase using 4-MU-Gal was 3.8-4.5. By contrast, liver GM1-beta-galactosidase gave a sharp activity peak at pH 4.2 with [3H]GM1 ganglioside. Inhibition by mercuric chloride and sensitivity to hydrogen peroxide and persulfate suggest the involvement of a sulfhydryl in catalysis.
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PMID:Purification and characterization of GM1 ganglioside beta-galactosidase from normal feline liver and brain. 41 73

Lactoperoxidase catalyzes the oxidation of thiocyanate by hydrogen peroxide and an intermediary product is formed with antibacterial properties. The components of this system, with the exception of hydrogen peroxide, are present in milk. H2O2 may be introduced by means of enzymatic generation and thus make the system complete. A two-enzyme system consisting of beta-galactosidase and glucose oxidase has been developed for this purpose. The coupled enzyme reaction is shown to work with high efficiency at the neutral pH of milk although the enzymes as such, particularly lactases suitable for immobilization, have optimal activities at much lower pH values. The results indicate that the lactoperoxidase system may in this way be employed to inactivate bacteria present in milk.
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PMID:An immobilized two-enzyme system for the activation of the lactoperoxidase antibacterial system in milk. 98 68

In Azotobacter chroococcum the hydrogenase structural genes (hupSL) cover about 2.8 kb of a 15-kb region associated with hydrogen-uptake (Hup) activity. Two other genes in this region, hupD and hupE, were located 8.9 kb downstream of hupL and were shown to be essential for hydrogenase activity by insertion mutagenesis. A fragment of DNA beginning 3.4 kb downstream of hupL was able to complement the hupE mutant, supporting earlier evidence for a promoter downstream of hupSL. Hybridization experiments showed that hupD and hupE share some similarity with a region of Alcaligenes eutrophus DNA which is apparently involved in the formation of catalytically active hydrogenase. The hupD gene encodes a 379-amino acid, 41.4-kDa polypeptide while hupE codes for a 341-amino acid, 36.1-kDa product. The predicted amino acid sequences of the hupD and hupE genes are homologous to the Escherichia coli hypD and hypE gene products, respectively. A polar mutation in hupD had no effect on beta-galactosidase activity in a strain also carrying a hupL-lacZ fusion, indicating that hupD and hupE are probably not involved in regulating hydrogenase structural gene expression.
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PMID:Characterization of two genes (hupD and hupE) required for hydrogenase activity in Azotobacter chroococcum. 152 70

An assessment was made of the efficacy of a beta-galactosidase, obtained from Aspergillus niger and added to intact milk, in decreasing lactose malabsorption and intolerance. Sixteen adult patients with malabsorption and intolerance to this sugar were studied in a double-blind crossover study vs. placebo. A 5-hour hydrogen breath test was used to assess malabsorption of lactose contained in 400 ml milk. When compared with placebo, the addition of exogenous lactase to intact milk caused a statistically significant reduction in the maximum breath H2 concentration (P less than 0.01) and in the cumulative H2 excretion (P less than 0.005). In the same way, the cumulative index for gastrointestinal intolerance was significantly lower (P less than 0.005) after the ingestion of lactase-added milk. This study demonstrates that enzyme replacement therapy, with beta-galactosidases obtained from Aspergillus niger, is effective in decreasing lactose malabsorption and its consequent intolerance in adult subjects with lactase deficiency.
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PMID:beta-Galactosidase from Aspergillus niger in adult lactose malabsorption: a double-blind crossover study. 154 16

The Escherichia coli beta-galactosidase enzyme was used as a reporter molecule for genetic fusions in Rhodobacter capsulatus. DNA fragments that were from the upstream region of the hydrogenase structural operon hupSLM and contained 5' hupS sequences were fused in frame to a promoterless lacZ gene, yielding fusion proteins comprising the putative signal sequence and the first 22 amino acids of the HupS protein joined to the eight amino acid of beta-galactosidase. We demonstrate the usefulness of the hupS::lacZ fusion in monitoring regulation of hydrogenase gene expression. The activities of plasmid-determined beta-galactosidase and chromosome-encoded hydrogenase changed in parallel in response to various growth conditions (light or dark, aerobiosis or anaerobiosis, and presence or absence of ammonia or of H2), showing that changes in hydrogenase activity were due to changes in enzyme synthesis. Molecular hydrogen stimulated hydrogenase synthesis in dark, aerobic cultures and in illuminated, anaerobic cultures. Analysis of hupS::lacZ expression in various mutants indicated that neither the hydrogenase structural genes nor NifR4 (sigma 54) was essential for hydrogen regulation of hydrogenase synthesis.
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PMID:Use of hupS::lacZ gene fusion to study regulation of hydrogenase expression in Rhodobacter capsulatus: stimulation by H2. 162 20

The activity of the mucosal beta-galactosidase of caecum and colon is low in both germfree and conventional rats. beta-Galactosidase activity occurs also in the chymus of germfree rats. It increases after monoassociation and is higher in conventional than in germfree animals. Lactose entering caecum and colon acts like dietary fibre and is hydrolysed mainly by the intestinal flora. Aerobe lactobacilli and bacteroides predominate in the microflora of rat caecum and colon. A lactose-containing diet increases the total number of germs and stimulates the growth of bifidobacteria. After special diets, rich in lactose and low in protein and phosphate (e.g. human milk and similar formulae), the number of bacteroides and other putrefactive germs decreases. Moreover, a lactose-containing diet alters the metabolic activity of intestinal microorganisms (activity of microbial beta-galactosidase, acidification and lowering of ph in the chymus, production of hydrogen, proteolytic activity.) Lactose as dietary fibre decreases the nitrogen excretion in the urine and increases the N-excretion in the faeces of conventional rats.
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PMID:[Lactose--a potential dietary fiber. The regulation of its microecologic effect in the intestinal tract. 3. Dietary fiber actions of lactose due to microbial activity]. 166 42

A cross-adaptive response (CAR), defined as a reduction of the effects of an agent by pretreatment with another agent, was demonstrated when E. coli WP2 cells were pretreated with hydrogen peroxide (H2O2) followed by challenging treatment with aldehyde compounds. Pretreatment with a sublethal dose (60 microM) of H2O2 for 30 min made WP2 cells resistant to the killing effects of formaldehyde (FA), and 4 other mutagenic aldehydes: glutaraldehyde, glyoxal, methyl glyoxal and chloroacetaldehyde. CAR was also observed in WP2uvrA (uvrA-) and ZA12 (umuC-) cells, but not in ZA60 (recA-) and CM561 (lexA- (Ind-] cells. A role of recA and lexA in CAR was further suggested by the lack of beta-galactosidase induction in recA- and lexA- cells by H2O2. CAR and beta-galactosidase induction, however, were found to be separate events since CAR was recovered by introducing the recA+ gene into lexA- cells, but no induction of beta-galactosidase by H2O2 was observed in cells with the same gene transfer. These results suggest that H2O2 has the capacity to induce a function which reduces the killing effects of aldehydes, and the function is controlled by the recA gene without involvement of SOS response.
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PMID:Cross-adaptive response in Escherichia coli caused by pretreatment with H2O2 against formaldehyde and other aldehyde compounds. 171 98

The effect of nonfermented dairy products containing yogurt or acidophilus cultures on lactose utilization by lactose-maldigesting humans was investigated. Yogurt and acidophilus milk containing 10(7) or 10(8) of Streptococcus thermophilus and Lactobacillus bulgaricus, or Lactobacillus acidophilus, respectively, were prepared using commercially processed 2% low fat milk. Immediately following inoculation, products were refrigerated. Lactose maldigestion was monitored by measuring breath hydrogen excretion at hourly intervals for 8 h following consumption of 400 ml of each test meal containing approximately 20 g of lactose. The yogurt milk containing 10(8) cfu/ml was shown to contain significant concentrations of microbial beta-galactosidase (EC 3.2.1.23; approximately 3 U/ml), which remained stable for at least 14 d at refrigerator temperatures. Breath hydrogen peaks were delayed and significantly lower (approximately 20 ppm at 5 to 7 h) than control values (approximately 70 ppm at 4 h), and intolerance symptoms were eliminated in all subjects. Yogurt milk containing 10(7) cfu/ml demonstrated intermediate breath hydrogen values and was marginally significantly different from control values. Lactobacillus acidophilus strains with varying resistance to bile and total beta-galactosidase-producing potential were also tested. Only one strain, LA-1, which demonstrated low bile resistance and intermediate beta-galactosidase activity, was capable of significantly decreasing breath hydrogen values when 10(8) cfu/ml of milk was consumed.
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PMID:Influence of nonfermented dairy products containing bacterial starter cultures on lactose maldigestion in humans. 190 36

Lactose in yogurt with live bacteria is better tolerated than lactose in other dairy foods, partly because of the activity of microbial beta-galactosidase (beta-gal), which digests lactose in vivo. To evaluate the ability of different strains and species of lactic acid bacteria to digest lactose in vivo, yogurts (containing mixtures of strains of Streptococcus salivarius subsp thermophilus and Lactobacillus delbrueckii subsp bulgaricus) and fermented milks (containing individual species of S thermophilus, L bulgaricus, L acidophilus, or Bifidobacterium bifidus) that varied in microbial beta-gal activity were produced. Selected products were fed to healthy people who cannot digest lactose, and breath hydrogen production was monitored. All yogurts dramatically and similarly improved lactose digestion, regardless of their total or specific beta-gal activity. The response to fermented milks varied from marginal improvement with B bifidus milk to nearly complete lactose digestion with L bulgaricus milk. The results suggest that total beta-gal was not the limiting factor in promoting lactose digestion, perhaps because of a limited rate of intracellular substrate transport.
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PMID:Strains and species of lactic acid bacteria in fermented milks (yogurts): effect on in vivo lactose digestion. 195 19

Lactose in yogurt is better digested than lactose in other dairy foods by lactase-deficient individuals, in part because of intraintestinal activity of yogurt microbial beta-galactosidase (beta-gal). The survival and activity of yogurt beta-gal depend on gastrointestinal transit, pH, and viability of the yogurt culture. To evaluate the ability of yogurt beta-gal to digest lactose when yogurt is consumed with food or with additional lactose, 22 healthy lactose-maldigesting individuals were fed 10 test meals. Results of breath-hydrogen expiration, incidence of symptoms, and enzyme and lactose content of gastric aspirates indicate that the consumption of a meal with yogurt does not inhibit, and may slightly improve, lactose digestion from yogurt. However, yogurt beta-gal appears unable to assist in the digestion of additional lactose beyond that normally present in yogurt.
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PMID:Lactose digestion from yogurt: influence of a meal and additional lactose. 202 Nov 32


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