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:3.2.1.20 (alpha-glucosidase)
4,237 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

The structure and the activity of acid phosphatase, beta-glucuronidase, alkaline phosphatase and ATP-ase in the liver and small intestine of rats receiving for 20 days a one-time, fixed at a certain time (2 o'clock) feeding was studied morphologically in dynamics in 2, 6, 24 and 48 hours after the last feeding. Furthermore, parallel with this the activity of acid phosphatase, beta-glucuronidase, alpha-glucosidase and beta-acetylglucosaminidase was determined in homogenates by biochemical methods. Alongside the total activity free activity of beta-acetylglucosaminidase and the activity of this enzyme in the blood plasma was defined. It is shown that during fasting, especially by the 48th hour, there takes place a significant activation of lysosomal enzymes both in the liver and in the small intestine (in the cells of the cylindrical epithelium). A significantly increased permeability of lysosomal membranes (mounting free activity of beta-acetylglucosaminidase) in the liver and of plasmic hepatocytes membranes (higher activity of the enzyme in the blood plasma) was also ascertained. The activation of the lysosomal enzymes is considered to be an adaptive reaction of the organism in fasting.
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PMID:[Histological, histoenzymatic and biochemical study of the liver and small intestine of rats during short periods of starvation]. 12 2

Renal epithelial function, proton flux and sodium stimulated proton flux, was observed in vesicles isolated from the brush border of the proximal tubule of Sockeye Salmon (Oncorhynchus nerka) during migration. Brush border membrane vesicles (BBMV) were isolated from the body kidney of Sockeye Salmon using aggregation/differential centrifugation techniques. Vesicle purity was tested using a series of epithelial and basal lateral markers including alkaline phosphatase, maltase, gamma-glutamyl transferase (GGTP), Mg(2+)-activated ATP-ase, Na(+)+K(+)-activated ATPase, and 5'-nucleotidase and the lysosomal marker acid phosphatase. An enrichment/depletion factor for each marker was determined by comparison of purified BBMV with kidney homogenate. Vesicles exhibit an enrichment factor for alkaline phosphatase, GGTP, maltase, Mg(2+)-activated ATP-ase, Na(+)+K(+)-activated ATPase, and 5'-nucleotidase. A depletion factor was observed for acid phosphatase. Vesicle integrity was tested by measuring the time course of proton flux in the presence of a pH gradient. Amiloride sensitive sodium stimulated proton flux was observed in these vesicles. The presence of sodium caused a saturable increase in the rate of proton flux, indicating the activity of a sodium/proton antiport protein in BBMV.
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PMID:Proton transport and Na+/H+ exchange in vesicles isolated from sockeye salmon (Oncorhynchus nerka) kidneys during migration from salt to fresh water. 132 4

Microbioassays using bacteria or enzymes are increasingly applied to measure chemical toxicity in the environment. Attractive features of these assays may include low cost, rapid response to toxicants, high sample throughput, modest laboratory equipment and space requirements, low sample volume, portability, and reproducible responses. Enzymatic tests rely on measurement of either enzyme activity or enzyme biosynthesis. Dehydrogenases are the enzymes most used in toxicity testing. Assay of dehydrogenase activity is conveniently carried out using oxidoreduction dyes such as tetrazolium salts. Other enzyme activity tests utilize ATPases, esterases, phosphatases, urease, luciferase, beta-galactosidase, protease, amylase, or beta-glucosidase. Recently, the inhibition of enzyme (beta-galactosidase, tryptophanase, alpha-glucosidase) biosynthesis has been explored as a basis for toxicity testing. Enzyme biosynthesis was found to be generally more sensitive to organic chemicals than enzyme activity. Bacterial toxicity tests are based on bioluminescence, motility, growth, viability, ATP, oxygen uptake, nitrification, or heat production. An important aspect of bacterial tests is the permeability of cells to environmental toxicants, particularly organic chemicals of hydrophobic nature. Physical, chemical, and genetic alterations of the outer membrane of E. coli have been found to affect test sensitivity to organic toxicants. Several microbioassays are now commercially available. The names of the assays and their basis are: Microtox (bioluminescence), Polytox (respiration), ECHA Biocide Monitor (dehydrogenase activity), Toxi-Chromotest (enzyme biosynthesis), and MetPAD (enzyme activity). An important feature common to these tests is the provision of standardized cultures of bacteria in freeze-dried form. Two of the more recent applications of microbioassays are in sediment toxicity testing and toxicity reduction evaluation. Sediment pore water may be assayed directly or solvents may be used to extract the toxicants. Some of the solvents used for extraction of organic chemicals are themselves toxic to bacteria (e.g., dichloromethane), requiring exchange with a less toxic solvent (e.g., ethanol, methanol, DMSO). A modification of the Microtox test allows direct assay of solid-phase samples such as sediments. The toxicity reduction evaluation (TRE) must be carried out at wastewater treatment plants whose effluents fail toxicity standards. The TREs require numerous and repeated toxicity assays, thus favoring application of microbioassays. Presently, no single microbioassay can detect all categories of environmental toxicants with equal sensitivity. Therefore, a battery of tests approach is recommended. The differential sensitivity of alternative tests may, in fact, be exploited. Further research is needed to construct strains of genetically engineered microorganisms or isolate microorganisms or enzymes that respond to specific classes of toxicants. These can be combined into batteries appropriate for different environments or test objectives.
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PMID:Bacterial and enzymatic bioassays for toxicity testing in the environment. 150 75

It has been suggested that alpha-glucosidase may be a marker of epididymal patency and function. Spermatozoal ATP concentrations decrease during passage through the epididymis, indicating efficient maturation. We correlated sperm motility with seminal plasma alpha-glucosidase activity and spermatozoal ATP. The sperm motility correlation with alpha-glucosidase activity was significantly positive, and the sperm motility correlation with spermatozoal ATP was significantly negative. It appears that high-alpha-glucosidase activity and low-spermatozoal ATP were present in semen with good sperm motility and could possibly indicate efficient epididymal function.
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PMID:alpha-Glucosidase, sperm ATP concentrations, and epididymal function. 187 46

Muscular glycogenosis is a disease resulting from genetic abnormalities altering an enzyme which is involved in glycogen metabolism. In addition to disorders of glycogenolysis and glycolysis, there are other pathological processes such as acid maltase (alpha-glucosidase) deficiency and diseases associated with abnormal glycogen structure. Glycolysis is the only metabolic pathway that can produce ATP in the absence of oxygen. It is then easy to understand that any disturbance in this energy pathway can result in dysfunction of the muscle machine and in a number of symptoms which are common to these abnormalities. An overall review of the various diseases know to exist on the glycogenolytic and glycolytic pathway will enable the reader to acquire a better knowledge of their particular features.
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PMID:[Muscular glycogenoses]. 189 12

Low spermatozoal ATP concentration in the presence of high alpha-glucosidase activity may indicate efficient epididymal function. It was suggested that detached ciliary tufts (DCTs) originated from the epididymis. We compared the spermatozoal ATP concentration and alpha-glucosidase activity in semen of patients with DCTs to that of a control group. Higher ATP concentration and lower alpha-glucosidase activity were found in patients with DCTs in their semen compared to the control group. These results might probably point out impaired epididymal function and further support the proposed epididymal origin of these tufts.
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PMID:Impaired epididymal function in patients with detached ciliary tufts in semen: a preliminary report. 195 21

Distal urinary acidification is thought to be mediated by a proton ATPase (H+-ATPase). We isolated a plasma membrane fraction from human kidney cortex and medulla which contained H+-ATPase activity. In both the cortex and medulla the plasma membrane fraction was enriched in alkaline phosphatase, maltase, Na+,K+-ATPase and devoid of mitochondrial and lysosomal contamination. In the presence of oligomycin (to inhibit mitochondrial ATPase) in the presence of ouabain (to inhibit Na+,K+-ATPase) and in the absence of Ca (to inhibit Ca2+-ATPase) this plasma membrane fraction showed ATPase activity which was sensitive to dicyclohexylcarbodiimide and N-ethylmaleimide. This ATPase activity was also inhibited by vanadate, 4,4'-diisothiocyano-2,2'-disulfonic stilbene and ZnSO4. In the presence of ATP, but not GTP or UTP, the plasma membrane fraction of both cortex and medulla was capable of quenching of acridine orange fluorescence, which could be dissipated by nigericin indicating acidification of the interior of the vesicles. The acidification was not affected by presence of oligomycin or ouabain indicating that it was not due to mitochondrial ATPase or Na+,K+-ATPase, respectively. Dicyclohexylcarbodiimide and N-ethylmaleimide completely abolished the acidification by this plasma membrane fraction. In the presence of valinomycin and an outward-directed K gradient, there was increased quenching of acridine orange, indicating that the H+-ATPase is electrogenic. Acidification was not altered by replacement of Na by K, but was critically dependent on the presence of chloride. In summary, the plasma membrane fraction of the human kidney cortex and medulla contains a H+-ATPase, which is similar to the H+-ATPase described in other species, and we postulate that this H+-ATPase may be involved in urinary acidification.
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PMID:Plasma membrane proton ATPase from human kidney. 287 34

A model of nonischemic hypoxia of the jejunum was designed in dogs, by shunting of blood from the inferior vena cava directly into the regional mesenteric arterial supply, thereby lowering the PaO2 of the blood that reached the jejunal wall from 98.6 +/- 3 to 62 +/- 5 mm Hg. Absorption rates of sodium, glucose, fructose, glycine, and the dibasic aminoacid lysine were studied by in situ luminal perfusion of a 30-cm proximal jejunal segment with a bicarbonate buffer solution containing phenol red as a nonabsorbable marker for determination of water fluxes. During periods of control, hypoxia, and after discontinuation of the venoarterial admixture (recovery), effluent perfusate was collected and mucosal biopsies were obtained for assay of lactase, maltase and sucrase activity, mucosal ATPase activity and ATP content, and for light- and electron microscopic examination. Mesenteric supply with hypoxic blood was associated with a significant inhibition of Na+,K+-ATPase activity (p less than 0.001) and a rise in mucosal ATP content (p less than 0.05). There was a significant reduction in the absorption rates of sodium (p less than 0.001), glucose, and glycine (p less than 0.01), but no change in the transport of fructose and of lysine. Brush border enzymes were unaltered. The histological appearance of the mucosa remained normal throughout the experiment, but on electron microscopy a distinct swelling of the enterocyte mitochondria was noted during the hypoxia period.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of nonischemic hypoxia on jejunal mucosal structure and function: study of an experimental model in dogs. 294 46

A technique for the isolation of intact brush borders from rabbit renal cortex was evaluated. The procedure was monitored by phase and electron microscopy and marker enzymes, i.e. ATP:NMN adenylyl transferase, nuclear; cytochrome oxidase, mitochondrial; beta-glucuronidase, lysosomal; and glucose-6-Pase, microsomal; and indicated an essentially pure preparation of brush borders. The disaccharidase, trehalase, previously reported in renal tubules, was localized uniquely in brush borders. Maltase was also found; the specific activities of the two enzymes in the brush borders were increased 10- to 20-fold. Other disaccharidases, such as sucrase, isomaltase, lactase, and cellobiase, were absent. It is suggested that trehalase and maltase are appropriate candidates for marker enzymes of the renal brush border. Isolated brush borders possessed a ouabain-sensitive (Na(+) + K(+)) ATPase, an oligomycin-insensitive Mg(++) ATPase, and a Ca(++)-activated ATPase. Alkaline phosphatases, dephosphorylating beta-glycero-P, and trehalose-6-P were also present. The specific activities of these enzymes were increased three-to-five fold in the brush-border preparations; however, activities were found in other subcellular fractions of the renal cortex. Hexokinase, although evident in the isolated brush border, was found prominently associated with other membranous fractions. Phosphoglucomutase and UDPG pyrophosphorylase were localized in the soluble fraction of the renal cortex.
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PMID:Isolation and biochemical characterization of brush borders from rabbit kidney. 425 Jun 12


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