Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An alpha-glucosidase was purified from baker's yeast. The molecular weight was approximately 44 000 daltons. SDS-disc gel electrophoresis suggested that the enzyme consisted of four subunits. The isoelectric point was at pH 5.4. The Km values for p-nitrophenyl alpha-D-glucopyranoside and maltose were 2.9 X 10(-4) and 2.5 X 10(-2) M, respectively. Binding of 2-(p-toluidino)naphthalene-6-sulfonate to the alpha-glucosidase was associated with a strong increase in fluorescence. The dissociation constant of the enzyme-TNS complex was 8 X 10(-5) M. The fluorescent probe did not interfere with the binding of glucose to the enzyme although the alpha-glucosidase was inhibited by high concentrations of TNS. The formation of an enzyme-glucose complex was indicated by an increase of fluorescence and by a shift in the wavelength for maximal emission which suggests that the binding process is associated with a change in conformation. The dissociation constant of the glucose--alpha-glucosidase complex KD = 0.57 X 10(-3) M, was calculated from the increase in fluorescence as a function of glucose concentration.
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PMID:On the properties of alpha-glucosidase and the binding of glucose to the enzyme. 36 Jul 36

A p-nitrophenyl-alpha-D-glucopyranoside-hydrolyzing alpha-glucosidase of a thermophile, Bacillus thermoglucosidius KP 1006, was purified to an electrophoretically-homogeneous state. Its molecular weight was estimated as 60 000 by gel electrophoresis. The molecular activity (ko) and the Km value at 60 degrees C and pH 6.8 for p-nitrophenyl-alpha-D-glucopyranoside were 233 s-1 and 0.24 mM, respectively. The enzyme cleft the non-reducing terminal alpha-1,6-glucosidic bonds of isomaltose, panose, isomaltotriose, isomaltotetraose, and isomaltopentaose. The ko values were 72.4, 194, 208, 233 and 167 s-1, and the Km values were 3.3, 9.5, 11, 13 and 21 mM, respectively. Each isomaltosaccharide was hydrolyzed to glucose by the cleavage of single glucose units from its nonreducing end. The present study suggests that the enzyme is an oligo-1,6-glucosidase (dextrin 6-alpha-glucanohydrolase, EC 3.2.1.10) and an exo-glucosidase.
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PMID:Hydrolysis of low molecular weight isomaltosaccharides by a p-nitrophenyl-alpha-D-glucopyranoside-hydrolyzing alpha-glucosidase from a thermophile, Bacillus thermoglucosidius KP 1006. 36 46

To determine whether oxytetracycline hydrochloride and the sodium salt of ampicillin have any adverse effects on the rat intestine, enteric enzyme levels and glucose transport rates were measured in vitro in rats. The intestinal transport of glucose did not differ significantly between control animals and those pretreated with ampicillin. For animals pretreated with oxytetracycline, the transport rates were significantly lower than those for the control group. The difference between the ampicillin and oxytetracycline groups, however, was not statistically significant. No significant differences in enteric levels of sucrase and maltase activity were found between any of the groups. The possibility that some antimicrobial agents may interfere with the absorption of nutrients suggested the need for caution in using these drugs in experimental animals.
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PMID:The effects of selected antimicrobials on glucose transport in the rat intestine. 37 63

In blind studies the effects of a new alpha-glucosidase inhibitor (BAY g 5421) were tested in normal weight and overweight male volunteers after oral application of 75, 150, or 300 mg of BAY g 5421 or placebo per os before three standardized main meals of one day. Before and three hours after each meal blood glucose, serum insulin, and serum triglyceride levels were determined. In addition, safety studies were performed. BAY g 5421 induced a statistically significant, in part dose-dependent inhibition of the postprandial increase of blood glucose- and serum insulin levels. The reduction of the postprandial increase of serum triglyceride levels was variable. Routine blood chemistry and hematology tests have revealed no adverse side effects; but the application of the drug was frequently associated with intestinal effects, such as flatulence and diarrhea, which were substrate (carbohydrate) and, in part, dose-dependent.
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PMID:The effects of the alpha-glucosidase inhibitor BAY g 5421 (Acarbose) on meal-stimulated elevations of circulating glucose, insulin, and triglyceride levels in man. 37 42

In a double-blind quadruple cross-over study the effect of a new alpha-glucosidase inhibitor (BAY g 5421) on postprandial blood glucose, serum insulin, and serum triglyceride increases was tested in 24 male healthy volunteers. They received before a standardized breakfast 50, 100, or 200 mg of BAY g 5421 or a placebo per os. The dose-time-response relationships were calculated and the drug tolerance was assessed. There was a statistically significant inhibition of the postprandial increases of the blood glucose, serum insulin, and triglyceride values. Further analysis showed no dose-dependent effect of the drug on the blood glucose values, whereas the serum insulin and triglyceride values were affected in a dose-dependent fashion. The maximal inhibitory effect on the serum insulin levels occurred 69 min after breakfast and on the serum triglyceride levels 104 min after breakfast. One hundred and 200 mg of BAY g 5421 were equally inhibitory-effective on the serum insulin levels, whereas the highest dose used was markedly more effective on serum triglyceride values than lower doses. Based on these results, a dosage of 100--200 mg of BAY g 5421/meal is recommended for clinical trials in metabolic diseases.
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PMID:The effects of the alpha-glucosidase inhibitor BAY g 5421 (Acarbose) on postprandial blood glucose, serum insulin, and triglyceride levels: dose-time-response relationships in man. 37 43

The enzymatic method of H. W. Schiwara (1972) Z. Klim. Chem. Klin. Biochem. 10,12--16 (reagents by Smith Kline Instruments), using the enzymatic reaction sequence alpha-amylase -- alpha-glucosidase -- hexokinase/glucose 6-phosphate dehydrogenase for the determination of alpha-amylase was evaluated on the ABA-100. The coefficient of variation for control sera and human pooled serum was 0.9--4.2% within series, and 1.4--6.6% day to day. Reference values for a healthy population (212 blood donors) in sera were 13--79 U/1 (+/- 2 SD), mean 46 U/1. In catch urines the values did not show a normal distribution; the minimal and maximal range for men was 58--385 U/1, for women 7--318 U/1. The kinetic curve of the enzymatic test was measured and the influence of glucose and linearity studied. In comparison with the enzymatic test, the chromogenic method Amlyochrom Roche was tested on the sera and urine of patients. The coefficient of correlation in sera was r = 0.975, in urine r = 0.965.
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PMID:[Determination of alpha-amylase by an enzymatic kinetic method on the ABA-100 (author's transl)]. 37 66

The major maltase activity was found in the kidneys, followed by liver, muscle and blood. Only low maltase activity has been found in adipose tissue, muscle, and brain. The pH-optimum of kidney maltase was at pH = 6.0, the Michaelis-Menten Constant was measured to be 15.6 X 10(-3) mol/l. Even with a dose of 200 mg maltose/100 g body weight saturation of the hydrolysing system could not be attained in living rats. In nephrectomized rats the maltose oxidation was reduced to 55%. Only 0.2% of the applied maltose is excreted into the bile. According to our results the following main pathway of metabolism of maltose is suggested: glomerular filtration of maltose, hydrolysis of maltose to glucose by maltases which are localized in the membrane of the kidney brush borders, absorption of glucose, oxidation of glucose to CO2. In addition an extrarenal maltase activity is considered in the liver. The metabolism of injected trehalose was only 10% when compared with the metabolism of maltose.
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PMID:[Localization of the degradation of injected maltose]. 39 62

Clinical isolates of Neisseria gonorrhoeae from Manitoba were tested for their carbohydrate degradation activity in Cystine Trypticase Agar (C.T.A) medium, Mueller-Hinton Agar and guinea pig serum agar. Each isolate was tested using 2 carbohydrates (e.g. glucose and maltose) in the above three media. Out of 661 isolates tested, only 80% were positively identified in C.T.A. medium. Mueller-Hinton agar allowed 88% identification while guinea pig serum agar yielded 100% identification. In a second series of experiments, 102 cultures of N. gonorrhoeae were used to compare Flynn & Waitkins medium with guinea pig serum agar. Only 91 of these were identified with Flynn and Waitkins medium while guinea pig serum agar identified all the 102 isolates. Guinea pig serum provides adequate growth of fastidious N. gonorrhoeae essential for detecting specific enzymes. Since guinea pig serum does not contain maltase activity, it does not interfere with the biochemical activities tested. Guinea pig serum agar is easy to prepare, does not require a heavy inoculum and gives definite color change in the medium.
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PMID:Neisseria gonorrhoeae identification in carbohydrate medium containing guinea pig serum. 40 82

To identify the site of stimulation of sucrase by a sucrose diet, changes in sucrase-specific activity of jejunal mucosa were studied after introduction of sucrose diet to carbohydrate-deprived rats. Results were correlated with simultaneous changes in villus gradients of sucrase-specific activity. Simultaneous with the introduction of sucrose diet, [(3)H]thymidine (100 muCi) was administered intravenously, and rates of cell migration measured during adaptation to the new diet. After a 72-h fast, rats fed sucrose diet for 6, 12, or 18 h showed no change in sucrase-specific activity in either whole mucosa or villus gradients. However, within 18-24 h after starting a sucrose diet, there was a marked rise in whole mucosal sucrase-specific activity above fasting values (99 +/- 14 vs. 38 +/- 4 muM glucose/min per g protein, P < 0.001) in association with the development of a region of increased activity at the lower villus (154 +/- 22 vs. 60 +/- 9 muM glucose/min per g protein, P < 0.02, but with no change in villus tip activity (56 +/- 5 vs. 46 +/- 8 muM glucose/min per g protein). Similar changes were seen in animals fed 24 h of sucrose diet after a 72-h carbohydratefree diet. Fasted animals fed sucrose diet for 36 h had increased sucrase-specific activity at the villus tip (144 +/- 11 muM glucose/min per g protein) as well as at the lower villus region, and this pattern persisted at 1 wk of sucrose diet. Maximal activity patterns for isomaltase and maltase paralleled those for sucrase, but the villus gradients for lactase were unaffected by sucrose diet. The region of maximal sucrase-specific activity always coincided with or followed the leading edge of radioactivity as determined by liquid scintillation counting. Therefore, sucrose-mediated changes in sucrase activity of the jejunal mucosa in the rat appear to be initiated at the level of the crypt epithelial cell and are expressed after a latent period of 18-24 h during which these cells mature and migrate toward the villus tip.
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PMID:Site of substrate stimulation of jejunal sucrase in the rat. 47 72

The present studies were undertaken to investigate the possible mechanism(s) of action of 2,2-dimethyl-1-(4-methylphenyl)-1-propanone (SaH 50-283) on food efficiency in rats. SaH 50-283, unlike phenformin (DBI), did not inhibit glucose absorption. However, hyperglycemia induced by oral maltose, lactose or starch load was markedly inhibited in animals pretreated with SaH 50-283. The ED25 for lowering blood sugar levels following an oral maltose load was calculated to be 12 mg/kg. SaH 50-283 could be administered as long as 7 hr prior to a maltose load and still maintain its effect. Food efficiency was significantly (P less than .01) lowered in rats pretreated with SaH 50-283 1 hr prior to a 2 hr feeding period of a purified high carbohydrate diet. It was concluded that the lowering of maltase activity in the brush border of animals treated with SaH 50-283 could partially account for its mechanism of action in lowering food efficiency in rats.
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PMID:The influence of 2,2-dimethyl-1-(4-methylphenyl)-1-propanone (SaH 50-283) on food efficiency in rats. 48 87


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