Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: T02G6 .1
 572,118 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sequential determinations of glucose outflow and inflow, and rates of gluconeogenesis from alanine, before, during and after insulin-induced hypoglycemia were obtained in relation to alterations in circulating epinephrine, norepinephrine, glucagon, cortisol, and growth hormone in six normal subjects. Insulin decreased the mean (+/-SEM) plasma glucose from 89+/-3 to 39+/-2 mg/dl 25 min after injection, but this decline ceased despite serum insulin levels of 153+/-22 mul/ml. Before insulin, glucose inflow and outflow were constant averaging 125.3+/-7.1 mg/kg per h. 15 min after insulin, mean glucose outflow increased threefold, but then decreased at 25 min, reaching a rate 15% less than the preinsulin rate. Glucose inflow decreased 80% 15 min after insulin, but increased at 25 min, reaching a maximum of twice the basal rate. Gluconeogenesis from alanine decreased 68% 15 min after insulin, but returned to preinsulin rates at 25 min, and remained constant for the next 25 min, after which it increased linearly. A fourfold increase in mean plasma epinephrine was found 20 min after insulin, with maximal levels 50 times basal. Plasma norepinephrine concentrations first increased significantly at 25 min after insulin, whereas significantly increased levels of cortisol and glucagon occurred at 30 min, and growth hormone at 40 min after insulin. Thus, insulin-induced hypoglycemia in man results from both a decrease in glucose production and an increase in glucose utilization. Accelerated glycogenolysis produced much of the initial, posthypoglycemic increment in glucose production. The contribution of glycogenolysis decreased with time, while that of gluconeogenesis from alanine increased. Of the hormones studied, only the increments in plasma catecholamines preceded or coincided with the measured increase in glucose production after hypoglycemia. It therefore seems probable that adrenergic mechanisms play a major role in the initiation of counter-regulatory responses to insulin-induced hypoglycemia in man.
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PMID:The role of adrenergic mechanisms in the substrate and hormonal response to insulin-induced hypoglycemia in man. 0 91

Three litters of pigs were weaned at 21 days of age, and 3 others were left with the sow. Pigs were killed at 21, 23, 28, or 39 days of age. Weaned pigs exhibited anxiety, gastrointestinal dysfunction, and decreased rate of body weight gain. Plasma glucose or liver glycogen concentrations were not decreased by weaning. Adrenal gland weights and tyrosine hydroxylase (EC 1.14.3a), dopamine beta-hydroxylase (EC 1.14.2.1), phenethanolamine-N-methyl transferase (EC 2.1.1), and monoamine oxidase (EC 1.4.3.4) activities were increased after weaning. Adrenal catecholamine and cortisol levels and dopa decarboxylase (EC 4.1.1.26) and catechol-o-methyl transferase (EC 2.1.1.6) activities were not significantly altered, although some increases were indicated. Cranial cervical ganglionic choline acetyltransferase (EC 2.3.1.6) and tyrosine hydroxylase activities were increased after weaning. Weaning of swine at 21 days of age is a stressful experience, and many effects persist for at least 18 days; however, growth was no longer impaired 18 days after weaning.
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PMID:Sympathoadrenal Neurochemistry and early weaning of swine. 0 71

A mild oxidative stimulation of the hexose monophosphate pathway of human glucose-6-phosphate dehydrogenase (EC 1.1.1.49)-deficient erythrocytes (Mediterranean variant) causes a significant drop in NADPH. These results, other than to confirm that glucose-6-phosphate dehydrogenase deficiency is a product deficiency disorder, demonstrate that under oxidative stimulation glutathione reductase may become functionally impaired and GSSG cannot be reduced at a sufficient rate.
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PMID:NADP+ and NADPH in glucose-6-phosphate dehydrogenase-deficient erythrocytes under oxidative stimulation. 0 94

Two glycosulfatases [EC 3.1.6.3], I and II, were purified 31.3- and 33.9-fold respectively, from a crude extract of the liver of Charonia lampas. The purification was carried out by the following chromatographic procedures; phosphocellulose, Sephadex G-150, Concanavalin A-Sepharose and isoelectric focussing. The enzyme preparations obtained were practically free from arylsulfatase [EC 3.1.6.1] contamination. Both glycosulfatases are probably glycoproteins differing in their carbohydrate moieties. The molecular weights of glycosulfatase I and II were estimated to be about 112,000 and 79,000 respectively. They had the same optimum pH of 5.5, and the same Km value of 25.0 mM for glucose 6-sulfate.
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PMID:Two glycosulfatases from the liver of a marine gastropod, Charonia lampas. Partial purification and properties. 0 53

The degradation of neoagarotetraose and neoagarobiose by Cytophaga flevensis was investigated. The organism possesses an enzyme that hydrolyzes the tetramer by cleavage of its central beta-galactosidic linkage. The product of this reaction, neoagarobiose, is further hydrolyzed enzymatically to D-galactose and 3,6-anhydro-L-galactose. Both enzyme activities were localized in the cytoplasm. Attempts were made to partially purify the respective enzymes and although a 30-40 fold-purification was achieved, the final preparation contained both neoagarotetra-ase and neoagarobiase activities. Evidence was obtained that these activities were due to different enzymes. Neoagarotetra-ase is highly specific for oligosaccharides containing neoagarobiose units; the rate of hydrolysis is greatest with neoagarotetraose. It cannot hydrolyze pyruvated neoagarotetraose. Optimal conditions for its activity were pH 7.0 and 25 C. Neoagarobiase hydrolyzes only neoagarobiose and neoagarobiitol and optimal conditions for activity were pH 6.75 and 25 C. Both enzymes were inhibited by Ag+, Hg2+ and Zn2+ ions and by p-CMB, which indicates that thiol groups are present in their active centres. Both enzymes were induced by neoagaro-oligosaccharides and melibiose and were repressed when glucose was added to the medium. Neoagarobiase was also induced by D-galacturonic acid. In continuous culture, the rate of enzyme production was maximal at a dilution rate of 0.1 h-1.
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PMID:Characterization of the neoagarotetra-ase and neoagarobiase of Cytophaga flevensis. 0 1

The influence of temperature on glucose metabolism of a psychotrophic strain of Bacillus cereus was investigated. The pH of the growth medium and spore-forming frequencies of B. cereus varied when grown at 32, 20, or 7 C. Radiorespirometric analyses revealed that vegetative cells of B. cereus metabolized glucose by simultaneous operation of the Embden-Meyerhof-Parnas pathway and the pentose phosphate pathway. As the growth temperature decreased, glucose was metabolized with increased participation of the pentose phosphate pathway. The shift of cells grown at a higher temperature to a lower temperature increased the relative participation of the pentose phosphate pathway, whereas the shift of cells grown at low temperatures to a higher temperature had the opposite effect. Cells of late logarithmic phase grown at 20 and 7 C oxidized acetate by the tricarboxylic acid cycle reaction. However, cells grown at 32 C failed to oxidize acetate to CO2 to any appreciable extent. The extracellular products resulting from the metabolism of glucose decreased as the growth temperature was lowered. Organic acids were the major extracellular products of cultures grown at 32 and 20 C. Acetic acid, lactic acid, and pyruvic acid together accounted for 86.1 and 78.9% of extracellular radioactivity, respectively, at the two temperatures. The relative ratio of these three acids varied between the temperatures. Little or no acid accumulated at 7 C.
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PMID:Influence of growth temperature on glucose metabolism of a psychotrophic strain of Bacillus cereus. 0 3

The isolation and partial characterization of the acid proteases A1 and A2 (EC3.4.23.6) from Aspergillus oryzae grown on solid bran culture are described. The purified preparations were essentially homogeneous by several criteria including sedimentation analysis and polyacrylamide gel electrophoresis. The physiochemical properties of the proteases A1 and A2 were as follows (in the order: A1, A2): molecular weight: 63 000 & 32 000; sedimentation coefficient s20, w: 3.93 and 3.16 S; diffusion constant D20, w, 5.63 - 10(-7) and 8.61 - 10(-7) CM2/S, partial specific volume, v: 0.73 ml/g for both; nitrogen content: 16.30 and 13.42%; E1% 1 cm at 280 nm: 5.9 and 11.1. The two enzymes had the same pH optima in the acid pH range, and both activated bovine pancreatic trypsinogen. The enzymes were essentially of the same amino acid composition and immunologically cross-reacted with each other. The protease A2 contained little or no carbohydrate, whereas the protease A1 was glycoprotein, containing 49% carbohydrate comprising glucose, mannose, and galactose. These results suggest that the protein portion of acid protease A1 is the same as that of acid protease A2.
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PMID:Purification and characterization of the two molecular forms of Aspergillus oryzae acid protease. 0 38

An extracecular alpha-glucosidase (alpha-D-glucoside glycohydrolase, EC 3.2.1.20) of a thermophile, Bacillus thermoglucosidius KP 1006, was purified about 350-fold. The purified enzyme had a specific activity of 164 mumol of p-nitrophenyl-alpha-D-glucopyranoside hydrolyzed per min at 60 degrees C and pH 6.8 per mg of protein. The molecular weight was estimated at 55 000. The pH and temperature optima for activity were 5.0--6.0 and 75 degrees C, respectively. Below 40 degrees C, the activity was less than 4.5% of the optimym. The enzyme showed a high specificity for alpha-D-glucopyranoside. The maximal hydrolyzing velocity per substrate diminished in the order: phenyl-alpha-D-glucopyranoside, p-nitrophenyl-alpha-D-glucopyranoside, isomaltose, methyl-alpha-glycopyranoside. The respective Km values were 3.0, 0.23, 3.2 and 27 mM. The activity was trace for turanose, and not detectable for sucrose, trehalose, raffinose, melezitose, maltose, maltotriose, phenyl-alpha-D-maltoside, dextran, dextrin and starch. Tris, p-nitrophenyl-alpha-D-xylopyranoside, glucose and glucono-delta-lactone blocked competitively the enzyme with respect to p-nitrophenyl-alpha-D-glucopyranoside. The Ki values were 0.12, 0.14, 2.2 and 2.4 mM, respectively. The activity was affected by heavy metal ions, but insensitive to EDTA, p-chloromercuribenzoate and iodoacetate. The enzyme was stable up to 60 degrees C, and inactivated rapidly at temperatures beyond 72 degrees C. The pH range for stability was 4.0--11.0 at 31 degrees C, and 6.0--8.5 at 55.5 degrees C. At 25 degrees C, the enzyme failed to be inactivated in 45% ethanol, in 7.2 M urea, and in 0.06% sodium dodecyl sulfate, but the tolerance was extremely reduced at 60 degrees C.
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PMID:Purification and properties of extracellular alpha-glucosidase of a thermophile, Bacillus thermoglucosidus KP 1006. 0 45

The effect of endogenous and exogenous secretin on fasting plasma insulin and glucose concentrations in peripheral venous blood was studied. In 10 non-diabetic subjects intragastric instillation of 300 ml 0.1 mol/l hydrochloric acid increased the plasma secretin concentration significantly. This increment did not influence insulin or glucose concentration. Control experiments with intragastric instillation of 300 ml of isotonic saline did not influence the plasma concentration of secretin, insulin or glucose. In four other non-diabetic persons no significant changes were found in plasma insulin or glucose concentration during an i.v. infusion of pure natural porcine secretin in doses of 0.1, 0.3, 1.0 and 3.0 clinical units/kg/h. The results suggest that secretin is without effect on insulin secretion in the fasting normal subject.
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PMID:Plasma insulin concentration during physiological variations in immunoreactive plasma secretin. 0 64

A culture filtrate of Irpex lacteus (Polyporus tulipiferae) was fractionated initially by salting out with ammonium sulfate, and a cellulase [EC 3.2.1.4.] fraction with high Avicel-hydrolyzing activity (formerly called Avicelase) was extensively purified by a series of column chromatography procedures. This purified endo-cellulase showed a less random hydrolytic mechanism, and was obtained in a yield of 0.04% with respect to the starting material. Its specific activity was enhanced approximately 30 times over that of the starting material. The cellulase component showed a single peak on both ultracentrifugal and acrylamide disc electrophoretic analyses. Its molecular weight was estimated to be 56,000. It contained 12.2% carbohydrate; the major sugar constituents were glucose and mannose. Regarding the amino acid composition, the contents of aspartic acid and glycine were highest, followed by those of glutamic acid, serine, and theonine. The cellulase component was not markedly inhibited by most metal ions tested excepted for Hg2+. This purified endo-cellulase attacked a series of cellooligosaccharides, beta-cellobioside, CM-cellulose, and insoluble, cellulosic substrates. In the digests from insoluble substrates, glucose, cellobiose, cellotriose, and cellotetraose were detectable, but the amount of cellobiose was the largest by far. In constrast, cellobiose and glucose were produced in almost equal amounts from beta-cellobioside.
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PMID:Purification and properties of an endo-cellulase of avicelase type from Irpex lacteus (Polyporus tulipiferae). 0 37


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