Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The sugar absorption test is the usual test for measurement of intestinal permeability. After intestinal absorption of probe sugars the subsequently excreted sugars are measured in urine. We have developed four enzymatic methods for the measurement of the urinary concentration of the probe sugars mannitol, raffinose, lactose and sucrose. Mannitol, lactose and sucrose are directly measured on Hitachi 917 using mannitol dehydrogenase, beta-galactosidase and invertase, respectively, as enzyme reagents. Raffinose measurement needs a three hours preincubation with alpha-galactosidase, after which the liberated sucrose is measured. The analytical performances such as within- and between-run precision, linearity, lowest detection limit, interference of other sugars and comparison with a gas chromatographic method are described for the four methods. These methods are accurate an can easily be performed in any clinical laboratory.
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PMID:Assessment of intestinal permeability: enzymatic determination of urinary mannitol, raffinose, sucrose and lactose on Hitachi analyzer. 1263 47

Larval and adult Psacothea hilaris feed on mulberry wood and leaves, respectively. High levels of endogenous activity against the major dietary carbohydrates, cellulose, hemicellulose, starch and soluble sugars were secreted in the gut of larvae and adults. Activity against pectin was also high and multiple polygalacturonase (EC 3.2.1.15) components were secreted in the gut of larvae. One glycanase component, beta-EG1, which was primarily an endo-beta-1,4-glucanase (EC 3.2.1.4) and another, beta-EG2, which was mostly an endo-beta-1,4-xylanase (EC 3.2.1.8), were also secreted, while at least four additional components hydrolysed laminarin, lichenin and crystalline cellulose. The beta-glycosidase component beta-GD1 was associated with most of the beta-mannosidase (EC 3.2.1.25) and beta-xylosidase (EC 3.2.1.37) activity secreted in the gut of larvae, while another, beta-GD2, was a beta-glucosidase (EC 3.2.1.21), the activity of which was directed against cellobiose and other beta-linked disaccharides, and a beta-fucosidase (EC 3.2.1.38). A beta-galactosidase (EC 3.2.1.23), which did not hydrolyse lactose, was also secreted, as were distinct beta-N-acetylhexosaminidase (EC 3.2.1.52), trehalase (EC 3.2.1.28), alpha-L-arabinosidase (EC 3.2.1.55), alpha-galactosidase (EC 3.2.1.22) and a minimum of four alpha-glucosidase (EC 3.2.1.20) components, one of which was also likely to be associated with a peak of alpha-mannosidase (EC 3.2.1.24) activity. The alpha-glucosidase components varied in their specificity for alpha-linked disaccharides, but none was active against sucrose, which was hydrolysed by a beta-fructofuranosidase (EC 3.2.1.26) component. Overall average levels of activity in larvae were twice those of adults, but the secretion of individual carbohydrases in both was not regulated in response to the relative abundance of particular carbohydrate components in their respective diets.
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PMID:Diet and carbohydrate digestion in the yellow-spotted longicorn beetle Psacothea hilaris. 1277 Apr 76

The effects of diarrhoea on the activities of brush-border disaccharidases namely lactase (EC 3.2.1.23), maltase (EC 3.2.1.20) and sucrase (EC 3.2.1.48) of Sprague-Dawley strain albino rats were induced in the rats with mannitol while secretory diarrhoea was induced with Salmonella typhimurium after an initial treatment with streptomycin. The activities of the enzymes were significantly reduced by diarrhoea. The extent of reduction in enzyme activity varied in the different segment of the small intestine in all the groups. The jejuno-ileal region had more changes in enzyme activities than in the duodenum. Higher activity levels were observed for maltase than for lactase. In the osmotic diarrhoea model, lactase activity was significantly lowered (P < 0.05) in the experimental group from day 5 to 10. Maltase activity on the other hand was significantly lowered (P < 0.001) at the peak of diarrhoea. Sucrase activity was also lowered significantly (P < 0.025) in the experimental animals within the first 10 days of diarrhoeal induction. In the secretory diarrhoea model, lactase activity was similar in all the experimental groups except for the streptomycin-salmonella-treated groups and control (P < 0.05). Higher lactase activity levels were observed in the secretory diarrhoea model compared to level in the osmotic diarrhoea model. Maltase activity levels were also lowered significantly (P < 0.05) in the experimental animals. Streptomycin had no effect on the activity of maltase.
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PMID:Comparative effects of osmotic and secretory diarrhoea on brush-border disaccharide hydrolases in rat. 1597 34

We designed and synthesized polyhydroxylated pyrrolidines 1-12 from L-tyrosine, L-phenylalanine, and D-tyrosine through iodine-mediated intramolecular cyclization followed by Woodward-Prevost reaction. The synthetic polyhydroxylated pyrrolidines were identified with structure-based inhibitory activity and selective inhibitory activity against alpha-rhamnosidase. (2S,3S,4R)-deacetyl anisomycin 7 was the best inhibitor among the 12 polyhydroxylated pyrrolidines because it possesses the same stereoconfiguration at C1, C2, C3 as alpha-L-rhamnopyranoside. An investigation into the nature of the inhibition showed that the synthetic pyrrolidines are competitive inhibitors. They also did not have remarkable inhibitory activity against seven glycosidases (alpha-glucosidase, alpha-mannosidase, alpha-amylase, beta-glucosidase, beta-galactosidase, beta-amylase, and invertase).
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PMID:Alpha-rhamnosidase inhibitory activities of polyhydroxylated pyrrolidine. 1603 52

The utilization of mono-, di-, and oligosaccharides by Bifidobacterium adolescentis MB 239 was investigated. Raffinose, fructooligosaccharides (FOS), lactose, and the monomeric moieties glucose and fructose were used. To establish a hierarchy of sugars preference, the kinetics of growth and sugar consumption were determined on individual and mixed carbohydrates. On single carbon sources, higher specific growth rates and cell yields were attained on di- and oligosaccharides compared to monosaccharides. Analysis of the carbohydrates in steady-state chemostat cultures, growing at the same dilution rate on FOS, lactose, or raffinose, showed that monomeric units and hydrolysis products were present. In chemostat cultures on individual carbohydrates, B. adolescentis MB 239 simultaneously displayed alpha-galactosidase, beta-galactosidase, and beta-fructofuranosidase activities on all the sugars, including monosaccharides. Glycosyl hydrolytic activities were found in cytosol, cell surface, and growth medium. Batch experiments on mixtures of carbohydrates showed that they were co-metabolized by B. adolescentis MB 239, even if different disappearance kinetics were registered. When mono-, di-, and oligosaccharides were simultaneously present in the medium, no precedence for monosaccharides utilization was observed, and di- and oligosaccharides were consumed before their constitutive moieties.
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PMID:Substrate preference of Bifidobacterium adolescentis MB 239: compared growth on single and mixed carbohydrates. 1686 45

Saccharomyces cerevisiae NUD1 gene codes for a spindle pole body component and nud1 temperature-sensitive mutants arrest at 38 degrees C in late anaphase with a tendency for lysis. We found that addition of 10% sorbitol to the medium complemented the lytic phenotype, and determination of colony-forming units evidenced the viability of nud1 cells for at least 48 hours at 38 degrees C. The protein amount in cell-free medium increased at 38 degrees C, and evidence is presented that intact nud1 cells exported proteins in amounts 10-fold higher compared wild type strains. The observed high amounts of extracellular acid phosphatase, invertase, and bacterial beta-galactosidase suggested the export of secretory proteins. This was evidenced by construction of nudlsec mutants and the observation that interruption of the secretory pathway resulted in absence of protein export at 38 degrees C. Proteins were exported through a cell wall showing increased porosity at 38 degrees C. The extracellular release of Gas1p and the facilitated transformability with plasmid DNA of nud1 cells indicated alternations of their cell walls at 38 degrees C. The export of proteins depends on oxidative phosphorylation as evidenced by disruption of the COX10 gene. Experiments with inhibitors of mitochondrial functions showed that the synthesis of adenosine triphosphate, but not the electron transport along the respiratory chain, has a key role in the export of proteins. The data show that the phenotype of S. cerevisiae nud1 mutants is characterized by enhanced export of secretory proteins and that the passage of proteins through the walls of nud1 cells is an active process.
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PMID:Enhanced protein export in Saccharomyces cerevisiae nud1 mutants is an active process. 1707 69

A method is described for the measurement of dietary fibre, including resistant starch (RS), non-digestible oligosaccharides (NDO) and available carbohydrates. Basically, the sample is incubated with pancreatic alpha-amylase and amyloglucosidase under conditions very similar to those described in AOAC Official Method 2002.02 (RS). Reaction is terminated and high molecular weight resistant polysaccharides are precipitated from solution with alcohol and recovered by filtration. Recovery of RS (for most RS sources) is in line with published data from ileostomy studies. The aqueous ethanol extract is concentrated, desalted and analysed for NDO by high-performance liquid chromatography by a method similar to that described by Okuma (AOAC Method 2001.03), except that for logistical reasons, D-sorbitol is used as the internal standard in place of glycerol. Available carbohydrates, defined as D-glucose, D-fructose, sucrose, the D-glucose component of lactose, maltodextrins and non-resistant starch, are measured as D-glucose plus D-fructose in the sample after hydrolysis of oligosaccharides with a mixture of sucrase/maltase plus beta-galactosidase.
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PMID:An integrated procedure for the measurement of total dietary fibre (including resistant starch), non-digestible oligosaccharides and available carbohydrates. 1761 81

Actinoplanes missouriensis (for glucose isomerase), Kluyveromyces fragilis (for beta-galactosidase), and Saccharomyces cerevisiae (for invertase) cells were successfully entrapped within cellulose and cellulose di- and triacetate beads employing several carried solvent systems. Cellulose beads prepared using a melt of dimethylsulfoxide (DMSO) and N-ethylpyridinium chloride (NEPC), or cellulose diacetate using a mixture of acetone and DMSO as solvent, were found to be promising as carriers for the invertase system, cellulose triacetate beads with DMSO as solvent for yeast beta-galactosidase, and cellulose beads with a melt of DMSO and NEPC as solvent for glucose isomerase. The kinetic behavior of A. missouriensis glucose isomerase whole cell cellulose beads in a plug-flow column reactor was studied as an example system in greater detail.
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PMID:Preparation and kinetic behavior of immobilized whole cell biocatalysts. 1794 48

A poly(acrylic acid)-polyethylene graft copolymer was prepared and used initially to couple to acid phosphatase, using soluble carbodiimides. Yields which were quite good were obtained with CMC but not with EDAC. The copolymers was used to couple trypsin using EEDQ. Several organic solvents were investigated for the preparation of the "activated" poly(acrylic acid) intermediate. Using the activated system, high concentrations of trypsin were bound but the relative activities were not very high. The yield was good with bovine serum albumin (BSA). When the method was used for invertase, acid phosphatase, and alkaline phosphatase, the yields were poor and the copolymer was shown to absorb protein by an ion-exchange mechanism. However, the activated system gave a good yield of coupling to phenylpropylamine. A polyethylene-coacrylic-acid polymer containing 13% of acrylic acid (by weight) was then converted to the acid chloride by refluxing with thionyl chloride. The chlorinated copolymer which contained 0.7% chlorine and a thionyl-chloride-treated polyethylene control which contained no chlorine were investigated in immobilization studies. Such coupling involved bovine serum albumin (BSA), alkaline phosphatase, trypsin, beta-galactosidase, and invertase. Bovine serum albumin coupled well to the support, but none of the enzymes gave high levels of enzymes activity. Phenylpropylamine coupled well and all of the acid chloride groups were involved. Tyrosine reacted with 63% of the available acid chloride groups.
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PMID:The immobilizaton of enzymes, bovine serum albumin, and phenylpropylamine to poly(acrylic acid)-polyethylene-based copolymers. 1854 30

Spherical beads of kappa-carrageenan containing entrapped cells were prepared in a two-step process. First, the beads were formed by dispersing a warm carrageenan cell suspension into stirring oil. After cooling (gelation) the beads were cured by treatment with amines. Ten amines of various sizes and structures were tested. We evaluated the mechanical strength and the applicability of aminetreated gels as immobilization matrices. The results of critical compression tests indicate that linear and branched polyethylenimines (PEI) are both good curing agents. PEI treated carrageenan beads also exhibited superior resistance to heat and abrasion. Furthermore, PEI polymers were demonstrated to be effective in stabilizing the lactase activity of the free and immobilized Bacillus stearothermophilus cells. The immobilized cell preparations of Saccharomyces cerevisiae, B. stearothermophilus, and Flavobacterium sp. were treated with branched PEI and evaluated for the activity of invertase (EC 3.2.1.26), lactase (EC 3.2.1.23), and glucose isomerase (EC 5.3.1.18), respectively, in a packed bed reactor at 60 degrees C. The apparent half-lives were 108, 39, and 64 days, respectively.
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PMID:Stabilization of kappa-carrageenan gel with polymeric amines: Use of immobilized cells as biocatalysts at elevated temperatures. 1856 Dec 17


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