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:2.7.1.1 (hexokinase)
5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Seven subjects were fed a 3,000 kcal defined formula diet daily for 19 days. Except for one 5-day period, 50% of the total caloric intake was provided as either oral or intravenous glucose. The study was divided into four periods as follows: period I lasted 5 days and provided 50% of calories as glucose; period II lasted 5 days and provided no carbohydrate (70% fat and 30% protein); period III lasted 4 days and provided 50% of calories as intravenous glucose and 50% of calories as oral fat plus protein; period IV lasted 5 days and provided 50% of calories as oral glucose. Intestinal biopsy specimens were taken on days 3 and 5 of each period, except period III when biopsies were done only on day 4. No change in intestinal morphology occurred during the study. The carbohydrate-free diet caused the alpha-glucosidase (maltase and sucrase) activities to decrease significantly from that seen with the glucose diet. Sucrase decreased from 14.4 +/- 1.0 to 7.1 +/- 0.9 mumoles/min per g tissue and maltase decreased from 56.1 +/- 3.4 to 30.0 +/- 2.1 mumoles/min per g tissue. Glycolytic enzyme activities decreased during the carbohydrate-free period (pyruvate kinase decreased from 236 +/- 12 to 78 +/- 8, fructose 1-phosphate aldolase decreased from 147 +/- 6 to 53 +/- 4, fructose-1,6-diphosphate aldolase decreased from 151 +/- 8 to 55 +/- 3, and hexokinase decreased from 21 +/- 3 to 7 +/- 1 nmoles/min per mg protein, respectively). Intravenous glucose caused no change in disaccharidase activities. The enzyme activities during periods I and IV were identical and significantly higher than during period II with the exception of fructose-1,6-diphosphatase which increased during period II as compared with periods I and IV. These findings provide an explanation for the transient period of decreased tolerance to dietary sugars when patients are weaned from total parenteral feedings to enteral feedings.
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PMID:Comparison of the adaptive changes in disaccharidase, glycolytic enzyme and fructosediphosphatase activities after intravenous and oral glucose in normal men. 17 Aug 20

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

Streptozotocin treatment (125 mg/kg) in the Chinese hamster induced hyperglycaemia, hypoinsulinaemia, hyperglucagonaemia and changes in body, liver, pancreas, stomach, kidney and adipose tissue weights. The pancreatic reserves of insulin and glucagon in the diabetic animals were low, but stomach glucagon high. These animals showed high levels of phosphoenolpyruvate carboxykinase and low levels of glucokinase, hexokinase, isocitrate dehydrogenase and malic enzyme, but normal levels of pyruvate kinase in the liver. Increases in lactate dehydrogenase subunit B and isozymes 2, 3 and 4 were also observed in the liver, but not in the epididymal fat pad, of the diabetic animals. N-Acetyl-beta-D-glucosaminidase was elevated in plasma, liver and heart, but not in the kidney of the treated animals. Renal alpha-galactosidase and beta-glucosidase were depressed, whereas beta-galactosidase and alpha-glucosidase remained essentially normal. These features indicated that there were considerable differences between the biochemical disorders associated with streptozotocin-diabetes in the Chinese hamster and the published observations in the rat.
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PMID:Streptozotocin-induced diabetes in the Chinese hamster. Biochemical and endocrine disorders. 59 Jun 51

An enzymatic method for the determination of maltose in blood is described. In this method after neutral deproteinization the assay is carried out by the hexokinase technique [6--7] after splitting of the maltose with alpha-glucosidase [8]. This time-saving procedure of high specificity and sensitivity requires only small volumes of blood. The practicability of the method is shown by analysis of blood level during an infusion of maltose.
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PMID:[The enzymatic determination of maltose in blood (author's transl)]. 92 10

Yeast strains bearing a deficiency in trehalose-6-phosphate synthase activity are unable to accumulate trehalose on any carbon source unless they contain one of the MAL genes. If the gene is inducible then synthesis of trehalose occurs specifically during growth on maltose: when the MAL gene is constitutive then trehalose accumulation can also be seen when cells are grown on glucose. Different systems for trehalose synthesis were suggested: one of them would require the UDPG-linked trehalose synthase whereas the second would utilize an alternative pathway. We proposed a mechanism by which the gene-product of a MAL gene would serve as a common positive regulator for the expression of the genes coding for maltose permease, alpha-glucosidase and some component of the trehalose accumulation system. In order to elucidate this novel pathway a strain lacking UDPG-linked trehalose synthase activity and harboring a defect in maltose uptake was constructed. Excessive maltose uptake resulted in accumulation of intracellular maltose, and twice as much trehalose as in a control strain. Partial inhibition of hexokinase by xylose affected the ratio between internal maltose and trehalose and significantly reduced glycogen synthesis. Sodium fluoride also blocked glycogen synthesis but allowed for trehalose accumulation. Moreover, a mutant which lacks hexokinase I and II was unable to accumulate trehalose when grown on glucose in spite of the presence of a constitutive MAL2 gene. These results suggest that trehalose synthesis would require G-6-P formation derived from maltose. Such a deviation would allow for slowing down the glycolytic flux which, in turn, would favour efficient maltose utilization.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Further evidence for the alternative pathway of trehalose synthesis linked to maltose utilization in Saccharomyces. 344 33

An enzymatic assay for the determination of alpha-amylase in serum was developed which employed a soluble substrate, maltoheptaose, and a coupled enzymatic indicator reaction consisting of alpha-glucosidase and the hexokinase-glucose-6-phosphate dehydrogenase system. We used high-performance liquid chromatography (HPLC) to establish the action pattern of maltoheptaose under the test conditions: (A) the action pattern of alpha-amylase, (B) that of the combined action of alpha-amylase and alpha-glucosidase. Conductive to this effect was: the availability of pure maltoheptaose and human pancreatic alpha-amylase; the development of an adequate procedure for sample pretreatment (partition chromatography on a mixed-bed ion exchange) and of an HPLC system for separation of substrate and reaction products without interference from by products of the assay (partition chromatography on a cation-exchange column with acetonitrile-water); and the use of a new, very sensitive refractometric detector revealing sugar amounts as low as 40 ng. We derived the following stoichiometric equations: (see formula index).
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PMID:Action pattern of human pancreatic alpha-amylase on maltoheptaose, a substrate for determining alpha-amylase in serum. 616 29

Most biological fluids contain both neutral and acid alpha-glucosidase. Optimal conditions were therefore developed for the selective determination of the activity of neutral and acid alpha-glucosidase, using 2-step, discontinuous assays. In the first step of the assay of neutral alpha-glucosidase, glucose was liberated from maltose (citrate-phosphate buffer, pH 6.8, 20 mmol/l maltose, 25 mmol/l turanose). Under these incubation conditions, turanose inhibited the residual activity of acid alpha-glucosidase almost completely without influencing the activity of neutral alpha-glucosidase. In the first step of the acid alpha-glucosidase assay, glucose was liberated from maltose (citrate-phosphate buffer, pH 3.8, 50 mmol/l maltose, 2 mol/l potassium chloride). Under these incubation conditions, potassium ions stimulate the activity of acid alpha-glucosidase and simultaneously inhibit almost completely the residual activity of neutral alpha-glucosidase. In the second step of the assay of neutral and acid alpha-glucosidase, the liberated glucose was measured by hexokinase/glucose-6-phosphate dehydrogenase. The effect of turanose and potassium ions on neutral and acid alpha-glucosidase from human urine was characterized.
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PMID:Selective determination of the activities of neutral and acid alpha-glucosidase using discontinuous assays. 635 65

Muscle hypertrophy was induced in the soleus muscle of young rats by tenotomy of the gastrocnemius and plantaris muscles. Three and 7 days afterwards the sciatic nerve was sectioned. The loss of weight of muscles subjected to this combined procedure three days after denervation was 30-40%. Lysosomal enzyme activities (acid phosphatase, alpha-glucosidase, beta-galactosidase and N-acetyl-beta-D-glucosaminidase) and energy enzyme activities (lactate dehydrogenase, LDH, triose-3-phosphate dehydrogenase, TPDH , D-hexokinase, HK and citrate synthase, CS) were determined 3 days after denervation, 3, 7 and 10 days after hypertrophy had been induced and 3 days after denervation of hypertrophying muscles on day 3 and 7. Normal non-operated rats of corresponding body weight served as controls and their enzyme activities were estimated on the same day. In the course of muscle hypertrophy, the 4 lysosomal enzyme activities increased progressively. Although 3 days' denervation of control muscles did not alter lysosomal enzyme activities, denervation of hypertrophying muscles greatly enhanced the activity of these enzymes. Enzymes of energy metabolism were affected to a lesser degree. The results suggest that denervation of hypertrophying muscles causes more extreme changes in muscle weight and lysosomal enzyme activities than denervation alone. The possible implications of this finding are discussed in relation to the rapid atrophy.
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PMID:Lysosomal and energy enzyme activities in hypertrophied rat soleus muscle after denervation. 671 25


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