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 production of dextransucrase from Leuconostoc mesenteroides NRRL B-512F was stimulated 2-fold by the addition of 0.005% of calcium chloride to the medium; levansucrase levels were unaffected. Dextransucrase was purified by concentration and dialysis of the culture supernatant with a Bio-Fiber 80 miniplant, and by treatment with dextranase followed by chromatography on Bio-Gel A-Fm. A 240-fold purification, with a specific activity of 53 U/mg, was obtained. Contaminating enzyme activities of levansucrase, invertase, dextranase, glucosidase, and sucrose phosphorylase were decreased to non-detectable levels. Poly(acrylamide)-gel electrophoresis of the purified enzyme showed only two protein bands, both of which had dextransucrase activity. These bands also gave a carbohydrate stain, indicating that the dextransucrase could be a glycoprotein. Acid hydrolysis, followed by paper chromatography, of the purified enzyme showed that the major carbohydrate was mannose. Concanavalin A completely removed dextransucrase activity from solution, confirming the mannoglycoprotein character of the enzyme. Dextransucrase activity was not altered by the addition of 0.008-4 mg/ml of dextran, but its storage stability was increased by the addition of 4 mg/ml of dextran. As previously shown by others, the activity of dextransucrase was decreased by EDTA, and was restored by the addition of calcium ions. Zinc, cadmium, lead, mercury, and copper ions were inhibitory to various degrees.
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PMID:Production, purification, and properties of dextransucrase from Leuconostoc mesenteroides NRRL B-512F. 10 66

The beta-fructofuranosidase from Kluyveromyces fragilis was purified to one band on electrophoresis by 3 different methods. Two of the preparations were found to be impure by isoelectric focusing. This demonstrates the need for more than one criteria of homogeneity when purifying this enzyme. The enzyme was found to be a glycoprotein, stable at 50 degrees C, with a pH optimum of 4.5. The cations Hg2+, Ag+, Cu2+ and Cd2+ exhibited a marked inhibition of the enzyme. Competitive inhibition was observed with the fructose analog 2,5-anhydro-D-mannitol suggesting that the enzyme is inhibited by the furanose form of fructose.
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PMID:Purification and properties of the beta-fructofuranosidase from Kluyveromyces fragilis. 688 6

Cadmium compounds are found widely in our environment: for example, in food, water, soil, and ambient air. The most important exposure route of animals to cadmium in the general environment is via oral exposure. In oral cadmium intoxication, the immediate target organ is the gastrointestinal tract. The aim of the present work was to determine how cadmium acts on the intestinal absorption of sugars and on the sucrase activity through rabbit jejunum, after in vitro administration and/or oral administration of CdCl2 in drinking water. Results obtained show that cadmium decreases D-galactose accumulation in the jejunum tissue. This effect seems to be the results of an action mainly located on Na(+)-dependent sugar transport of the mucosal border of the intestinal epithelium, because cadmium seems not to modify the sugar diffusion across the intestinal epithelium. Cadmium has also been shown to inhibit the (Na(+)-K+)-ATPase activity of the enterocyte, which might explain the inhibition of the D-galactose Na(+)-dependent transport. Nevertheless, a direct action of the cadmium molecule on the Na(+)-dependent carrier cannot be discarded. Cadmium altered the sucrose activity when it was administered in the drinking water for 4 d.
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PMID:Effect of cadmium on enzymatic digestion and sugar transport in the small intestine of rabbit. 750 39

In vitro and in situ findings suggest an impairment of digestive and absorptive functions in the small intestine by enteral cadmium salts. In the rat, diets with up to 1 mmol Cd/kg are well tolerated, however, so that the impairment might not be this drastic or compensated by adaptive changes. To elucidate whether small intestinal functions are altered, we studied the effect of dietary cadmium on the longitudinal pattern of mucosal enzymes and the in vitro uptake of methyl alpha-D-glucoside in the small intestine of female rats. Three groups of rats were employed, a control group and two groups receiving dietary CdCl2 either at 0.3 or 1.0 mmol Cd/kg of diet. Rats were killed after 1 week of feeding. The entire small intestine was removed, rinsed with ice-cold saline and divided into 12 segments of equal length. Mucosal scrapings from each segment were used to measure mucosal cadmium levels, sucrase, lactase, alkaline phosphatase, glycylleucine-hydrolase, and diamine oxidase activities. Sugar uptake was determined in vitro in all segments using everted rings tissue accumulation method. Although cadmium levels in the mucosa were high (>100 ng Cd/mg protein or >100 micromol Cd/kg WW) most enzyme activities were only slightly changed. When significant decreases in activity were detected, they were only observed in the proximal small intestine. Sugar uptake was also impaired only in proximal segments, the maximal transport capacity was reduced by approximately 20%. These findings suggest that cadmium even at dietary levels of 1 mmol/kg do not lead to a drastic impairment of digestive and absorptive functions in the small intestine and that in the rat presently observed, mostly proximal impairments are easily compensated by unaltered distal functions. Certainly, absorption of micronutrients, for which an impaired proximal function cannot be compensated, e.g. iron, might be critical in this respect.
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PMID:Longitudinal pattern of enzymatic and absorptive functions in the small intestine of rats after short-term exposure to dietary cadmium chloride. 1004 3

In vitro effects of cadmium (0.5-50 mg/l) and DDVP (0.2-100 mg/l) on the total amylolytic, sucrase and protease activities of intestinal mucosa have been studied for the first time in 11 freshwater teleosts. Total amylolytic activity in burbot, crucian carp and common carp, sucrase activity in blue bream and total proteolytic activity in burbot and pike were significantly decreased by cadmium at 50 mg/l. DDVP (at 0.2 mg/l) caused a significant decrease in total proteolytic activity in pike but had no effect on either protease or carbohydrase activities in other fish species.
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PMID:In vitro effects of cadmium and DDVP (dichlorvos) on intestinal carbohydrase and protease activities in freshwater teleosts. 1019 24

A cluster of genes involved in antibiotic and heavy metal resistance has been characterized from a clinical isolate of the gram-negative bacterium Stenotrophomonas maltophilia. These genes include a macrolide phosphotransferase (mphBM) and a cadmium efflux determinant (cadA), together with the gene cadC coding for its transcriptional regulator. The cadC cadA region is flanked by a truncated IS257 sequence and a region coding for a bin3 invertase. Despite their presence in a gram-negative bacterium, these genetic elements share a common gram-positive origin. The possible origin of these determinants as a remnant composite transposon as well as the role of gene transfer between gram-positive and gram-negative bacteria for the acquisition of antibiotic resistance determinants in chronic, mixed infections is discussed.
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PMID:Stenotrophomonas maltophilia D457R contains a cluster of genes from gram-positive bacteria involved in antibiotic and heavy metal resistance. 1085 30

Cadmium (Cd) uptake effects on sucrose content, invertase activities, and plasma membrane functionality were investigated in Rangpur lime roots ( CITRUS LIMONIA L. Osbeck). Cadmium accumulation was significant in roots but not in shoots and leaves. Cadmium produced significant reduction in roots DW and increment in WC. Leaves and shoots did not show significant differences on both parameters. Sucrose content was higher in control roots than in Cd-exposed ones. Apoplastic sucrose content was much higher in Cd-exposed roots than in control ones. Cd-exposed roots showed a significant decrease in both cell wall-bound and cytoplasmic (neutral) invertase activities; while the vacuolar isoform did not show any change. Alterations in lipid composition and membrane fluidity of Cd-exposed roots were also observed. In Cd-exposed roots phospholipid and glycolipid contents decreased about 50 %, while sterols content was reduced about 22 %. Proton extrusion was inhibited by Cd. Lipid peroxidation and proton extrusion inhibition were also detected by histochemical analysis. This work's findings demonstrate that Cd affects sucrose partitioning and invertase activities in apoplastic and symplastic regions in Rangpur lime roots as well as the plasma membrane functionality and H (+)-ATPase activity.
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PMID:Cadmium induces changes in sucrose partitioning, invertase activities, and membrane functionality in roots of Rangpur lime (Citrus limonia L. Osbeck). 1688 81

Seeds of pea (Pisum sativum L.) were germinated for 5d by soaking in distilled water or 5mM cadmium nitrate. The relationships among cadmium stress, germination rate, changes in respiratory enzyme activities and carbohydrates mobilization were studied. Two cell fractions were obtained from embryonic axis: (1) mitochondria, used to determine enzyme activities of citric acid cycle and electron transport chain, and (2) soluble, to measure some enzyme activities involved in fermentation and pentose phosphate pathway. Activities of malate- and succinate-dehydrogenases (MDH, SDH) and NADH- and succinate-cytochrome c reductases (NCCR, SCCR) were rapidly inhibited, while cytochrome c oxidase (CCO) was unaltered by cadmium treatment. However, this stimulated the NADPH-generating enzyme activities of the pentose phosphate pathway, glucose-6-phosphate- and 6-phosphogluconate-dehydrogenases (G6PDH, 6PGDH), as well as enzyme activity of fermentation, alcohol dehydrogenase (ADH), with concomitant inhibition in the capacity of enzyme inactivator (INADH). Moreover, Cd restricted carbohydrate mobilization in the embryonic axis. Almost no glucose and less than 7% of control fructose and total soluble sugars were available in the embryo tissues after 5d of exposure to cadmium. Cotyledonary invertase isoenzyme activity was also inhibited by Cd. The results indicate that cadmium induces disorder in the resumption of respiration in germinating pea seeds. The contribution of Cd-stimulated alternative metabolic pathways to compensate for the failure in mitochondrial respiration is discussed in relation to the delay in seed germination and embryonic axis growth.
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PMID:Respiratory metabolism in the embryonic axis of germinating pea seed exposed to cadmium. 1876 Apr 97

There is a growing concern on the potential application of a direct current (DC) electric field to soil for removing contaminants, but little is known about its impact on soil enzyme activities. This study investigated the change of enzyme activities of a heavy metal contaminated soil before and after electrokinetic (EK) treatments at lab-scale and the mechanisms of EK treatment to affect soil enzyme activities were explored. After treatments with 1-3 V cm(-1) of voltage gradient for 420 h, soil pH, electrical conductivity (EC), soil organic carbon, dissolved organic carbon (DOC), soil heavy metal concentration and enzyme activities were analyzed. The results showed that the average removal efficiencies of soil copper were about 65% and 83% without and with pH control of catholyte, respectively, and all the removal efficiencies of cadmium were above 90%. The soil invertase and catalase activities increased and the highest invertase activity was as 170 times as the initial one. The activities of soil urease and acidic phosphatase were lower than the initial ones. Bivariate correlation analyses indicated that the soil invertase and acidic phosphatase activities were significantly correlated with soil pH, EC, and DOC at P<0.05, but the soil urease activities had no correlation with the soil properties. On the other hand, the effects of DC electric current on solution invertase and catalase enzyme protein activities indicated that it had negative effect on solution catalase activity and little effect on solution invertase activity. From the change of invertase and catalase activities in soil and solution, the conclusion can be drawn that the dominant effect mechanism is the change of soil properties by EK treatments.
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PMID:Effects of electrokinetic treatment of a heavy metal contaminated soil on soil enzyme activities. 1973 75

Soils samples collected from five different areas (S1-S5) around electroplating industries in the city of Coimbatore were analysed for the activities of selected enzymes (cellulase, phosphatase, amylase, urease, and invertase) in the presence and absence of the earthworm Lampito mauritii (Kinberg). Heavy metal analysis of soils showed that chromium (<504 mg/kg) and copper (<28.1mg/kg) contents were much higher than cadmium (<10.60 mg/kg) except in S5, where cadmium (10.6 mg/kg) was higher than the copper. Except for phosphatase, the activities of all enzymes increased with increasing period of incubation under laboratory conditions, both with and without earthworms. The results of the three-way ANOVA (effect of three factors- worms-with and without addition, soil and incubation time), however, showed that there was no significant difference between enzyme activities (with and without earthworm) and soil and incubation time for amylase and urease activity. Further, no significant difference was found between soils for cellulase activity and between all the above factors for urease activity. The results concluded that though the earthworms died at the end of the incubation period, the resultant increase or decrease in the enzymatic activity may be attributed to the metabolic activities of the worms during their lifetime in the experimental container. Also, the worms after death may have provided suitable substrate for the growth of the microorganisms thereby influencing enzyme activity.
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PMID:Selected enzyme activities of urban heavy metal-polluted soils in the presence and absence of an oligochaete, Lampito mauritii (Kinberg). 2265 12


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