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)

The mechanism of starch degradation by the fungus Trichoderma viride was studied in strain CBS 354.44, which utilizes glucose, starch and dextrins but is unable to assimilate maltose. It was shown that the amylolytic enzyme system is completely extracellular, equally well induced by starch, amylose or amylopectin and that it consists mainly of enzymes of the glucoamylase type which yield glucose as the main product of starch hydrolysis. Small amounts of alpha-amylase are produced also. The enzymes produced in starch cultures degrade starch, amylose and amylopectin equally well. Enzyme synthesis in starch media takes place to a considerable extent after exhaustion of the carbon source when maximum growth has been attained. Low-molecular dextrins are degraded by extracellular enzymes of the glucoamylase type. These enzymes are produced in media containing starch or dextrins. Maltotriose is consumed for only one third leaving maltose in the culture filtrate. Maltose is hardly attacked and hardly induces any amylolytic enzyme activity. No stable alpha-glucosidase appears to be produced.
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PMID:Starch degradation by the mould Trichoderma viride. I. The mechanism of starch degradation. 1 Aug 32

The author reports a modification of the UV method UltraZyme Plus alpha-Amyl Harleco and the adaptation to the Eppendorf Enzymautomat 5010. alpha-amylase acts on an oligosaccharide mixture yielding maltose, which is hydrolysed by alpha-glucosidase. The liberated glucose is determined specifically by the hexokinase/glucose-6-phosphate dehydrogenase (NAD+-dependent) method+ by addition of pyruvate, lactate dehydrogenase and ATP. Thereafter the lactate dehydrogenase reaction is stopped by addition of oxamate and the alpha-amylase activity is measured.
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PMID:[Kinetic determination of alpha-amylase in serum and urine with an oligosaccharide as substrate--modification for a fully mechanized enzyme measuring device (author's transl)]. 9 28

I describe a new kinetic enzymatic saccharogenic method for assaying alpha-amylase in human serum and urine. alpha-Amylase liberates maltose from starch. This is successively acted on by alpha-glucosidase, mutarotase, and glucose dehydrogenase. The resulting conversion of NAD+ to NADH, measured at 340 nm, during a 20-min incubation reflects amylase activity. Endogenous glucose is destroyed before measurement of amylase activity is begun.
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PMID:New saccharogenic determination of alpha-amylase in serum and urine. 21 41

alpha-Amylase can be measured continuously with the aid of 4-nitrophenyl glucosides, especially 4-nitrophenyl maltotrioside; the large scale enzymatic synthesis of this compound seems to be possible. Another method, which does not suffer from interference by endogenous glucose, consists of the hydrolysis of maltotetraose by alpha-amylase, followed by the determination of maltose. The substrate and the auxiliary enzymes are, however, relatively expensive. Continous methods, based on the measurement of the glucose released by alpha-amylase, are more sensitive. However, they suffer from interference by blood sugar, with exception of mechanized procedures, which remove glucose by gel filtration of the sample. Moreover these methods need alpha-glucosidase, which degrades maltooligosaccharides consisting of less than seven glucose units, whereas higher polymerized substrates show slower degradation rates by amylase, and the kinetics are not easy to understand.
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PMID:alpha-Amylase assay: current state and future development. 31 93

The organism Bacillus amyloliquefaciens is capable of producing alpha-amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) and isoamylase (glycogen 6-glucanohydrolase, EC 3.2.1.68) extracellurlarly and a membrane-bound, intracellular alpha-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20). The amounts of alpha-glucosidase in cells of B. amyloliquefaciens grown on amylaceous polysaccharides were significantly higher then in cells grown on non-carbohydrate carbon sources. alpha-Glucosidase was exclusively found associated with membranes from ruptured spheroplasts by subcellular fractionation and solubilization studies. Salt solutions and chelating agents alone did not dislodge alpha-glucosidase from membranes, but in combination with detergents were most effective in solubilizing active enzyme (0.1% sodium cholate (pH 8.0)/0.4 M sodium chloride). Purified alpha-glucosidase very rapidly hydrolized p-nitrophenyl alpha-D-glucopyranoside and sucrose. Maltose, maltotriose, isomaltose and isomaltotriose were hydrolized at slower rates, whereas beta-glucosides and polymeric alpha-glucans were not attacked. Other properties of the purified enzyme were as follows: Temperature optimum for catalysis = 39 +/- 1 degrees C; pH optimum = 6.8; molecular weight = 27,000 +/- 1000. alpha-Glucosidase is proposed to function in the endogenous metabolism of alpha-glucans provided extracellularly as carbon sources for growth of B. amyloliquefaciens.
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PMID:alpha-Glucosidase, a membrane-bound enzyme of alpha-glucan metabolism in Bacillus amyloliquefaciens. Purification and partial characterization. 33 55

We described a partitioned enzyme-sensor system, which incorporates an immoblized substrate and three or more discrete immobilized enzymes. This instrument measures alpha-amylase activity by passing the solution containing alpha-amylase over a column packed with immobilized starch. The resulting oligosaccharides are successively exposed to a column or columns containing immobolized glucose oxidase, catalase, glucoamylase or maltase, and glucose oxidase. The resulting hydrogen peroxide is detected by a three-electrode amperometric cell. All immobilized reagents were immobilized on a particulate, porous alumina to allow rapid and constant flow rate. With use of less than optimum immobilized reagents, alpha-amylase activity has been measured from about 5 to 200 kU/liter with a 50 microliter sample size. Lack of sensitivity is predominantly attributable to the low activity and low stability of immobilized maltase and glucoamylase. We believe that a clinical test using this system is feasible and desirable because the immobilized reagent system should allow for testing of alpha-amylase with excellent precision, convenience to the operator, and low cost.
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PMID:Coupled reactions of immobilized enzymes and immobilized substrates: clinical application as exemplified by amylase assay. 35 22

We evaluated the Harleco alpha-glucosidase/hexokinase/glucose-6-phosphate dehydrogenase-coupled alpha-amylase method, bu use of the GEMSAEC centrifugal analyzer. Performance evaluation included kinetic studies of substrate and maltose hydrolysis as well as effects of endogenous glucose and fructose. The reagent was found to give a linear response with alpha-amylase activity to greater than 1200 U/liter. Within-run precision resulted in coefficients of variation (CV) of 0.9 to 3.2% over the range studied. Day-to-day precision corresponded to CV's of 2.4 to 4.4% over the same range of alpha-amylase procedure was found to be good (r = 0.997) for patients' sera examined.
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PMID:Enzyme-coupled ultraviolet determination of alpha-amylase activity with the GEMSAEC centrifugal analyzer. 35 41

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 kinetic studies on the reactions of human pancreatic and salivary alpha-amylases with several maltooligosaccharides (maltotetraose, maltopentaose, maltohexaose, and maltoheptaose) were carried out. The susceptibility to hydrolysis with human pancreatic alpha-amylase decreased in the order of maltopentaose, maltohexaose, maltotetraose, and maltoheptaose, while with human salivary alpha-amylase maltopentaose was hydrolysed slightly slower than maltohexaose but fairly faster than maltotetraose or maltoheptaose from a viewpoint of the rates of reactions based on the amount of substrate changed. The relative rates of production of substrates, utilized in the coupled yeast alpha-glucosidase reaction, increased in the order of maltoheptaose, maltohexaose, maltotetraose, and maltopentaose with human pancreatic alpha-amylase, while with human salivary alpha-amylase in the order of maltoheptaose, maltotetraose, maltohexaose, and maltopentaose. Thus, maltopentaose was considered to be the best substrate over maltotetraose, maltohexaose or maltoheptaose for the alpha-glucosidase coupled method of alpha-amylase determination.
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PMID:Action of human pancreatic and salivary alpha-amylases on maltooligosaccharides: evaluation of kinetic parameters. 38 76

Intestinal mucosa and pancreas from purebred Beagle dogs were assayed for carbohydrase activity, using several methods of tissue treatment. The enzymes found and studied were alpha-amylase, sucrase, lactase, amyloglucosidase, cellobiase, maltase, and isomaltase. Experiments using polyacrylamide gel columns and heat inactivation showed the presence of an isozyme of maltase which degrades isomaltose. This activity had not been previously demonstrated in dogs. An optimal standard procedure is presented for the preparation and assay of canine digestive enzymes. A statistical analysis of variance of the results showed that the variance was primarily associated with differences among dogs and not by variance within the procedure. When the different extraction procedures were used, results indicated that the level of enzymes detected differed with the method of treatment.
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PMID:Detection and definition of canine intestinal carbohydrases, using a standardized method. 88 14


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