Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

8 patients with chronic pyelonephritis were given gentamycin intramuscularly injected in individual dosage during 8-10 days. Here the behaviour of the excretion of protein, alanine aminopeptidase alkaline phosphatase, alpha-glucosidase, gamma-glutamyl transpeptidase and lysozyme with the urine was tested. With the exception of the lysozymuria, which increased only in patients with chronic renal insufficiency, regularly a hyperenzymuria developed. Most distinctly the excretion of the alanine aminopeptidase increased. After initial decrease the excretion of total protein transiently increased after completion of the gentamycin therapy. All the deviations were reversible. From the increased excretion of enzymes may not be concluded to a nephrotoxicity of gentamycin.
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PMID:[The effect of therapeutic gentamycin doses on the enzyme secretion in urine]. 0 Aug 56

Urinary excretion of lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase, beta-glucuronidase, and leucinearylamidase was studies in a carefully selected group of 100 healthy subjects, 50 women and 50 men. Enzyme activities were assayed in 3-h morning samples after gel filtration of the urine. Activities were related to time volume, and to urinary creatinine concentration. Several transforming functions had to be applied to enzyme output data to obtain an approximation to gaussian frequency distribution. Men showed a significantly higher excretion of gamma-glutamyltransferase, alpha-glucosidase, trehalase, N-acetyl-beta-glucosaminidase,beta-glucuronidase, and leucine arylamidase activity than did women if enzyme activity was related to urinary time volume. Women excreted more lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, alpha-glucosidase, trehalase, and N-acetyl-beta-glucosaminidase activity than did men, if urinary creatinine was used as the basis of reference. Reference intervals were calculated as 2.5 and 97.5 percentiles for both sexes.
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PMID:Normal limits of urinary excretion of eleven enzymes. 1 92

1. Highly sensitive technique are described for the assay of plasma membrane (5'-nucleotidase, alkaline phosphatase), microsomal (neutral alpha-glucosidase, leucyl-2-naphthylamidase) and biliary canalicular (gamma-glutamyltransferase) enzymes and for nine acid hydrolases (acid phosphatase, phosphodiesterase, beta-glucosidase, alpha-glucosidase, alpha-galactosidase, beta-galactosidase, alpha-mannosidase, N-acetyl-beta-glucosaminidase, beta-glucuronidase) in human liver. 2. Optimum and specific assay systems have been developed which give linear kinetics for all enzymes. 3. The range of enzyme activities in samples of human liver, obtained by closed needle biopsy, and sera have been determined.
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PMID:Enzyme activities in human liver biopsies: assay methods and activities of some lysosomal and membrane-bound enzymes in control tissue and serum. 1 4

The properties of seven enzymes were studied in extracts from Myxobacter AL-1. The enzymes were isocitrate dehydrogenase (E.C.1.1.1.42), succinate dehydrogenase (E.C.1.3.99.1), alkaline phosphatase (E.C.3.1.3.1), alpha-glucosidase (E.C.3.2.1.20), beta-glucosidase (E.C.3.2.1.21), beta-galactosidase (E.C.3.2.1.23), and N-acetyl-glucosaminidase (E.C. 3.2.1.30). Four of these enzymes: isocitrate dehydrogenase, alpha-glucosidase, beta-glucosidase, and beta-galactosidase are cytosolic enzymes. Succinate dehydrogenase was found to be located on the cytoplasmic membrane system, whereas alkaline phosphatase and N-acetylglucosaminidase were considered as enzymes which bind the outer membranes resp. the cell wall. During the cell cycle, all enzymes have a pattern of discontinuous activity increase. Succinate dehydrogenase and isocitrate dehydrogenase exhibit a stepwise increase of activity, whereas the other enzymes follow the pattern of a peak enzyme.
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PMID:Studies on the cell cycle of Myxobacter AL-1. II. Activities of seven enzymes during the cell cycle. 2 Aug 61

1. Enterocytes, isolated from the proximal jejinum and distal ileum of the rat, were homogenized and their organelles separated by isopycnic centrifugation on continuous sucrose density gradients. The distributions of marker enzymes for the principal organelles, RNA and protein were determined in the sucrose gradients and related to the activities per entercocyte. 2. In the jejunum the modal equilibrium densities of the various organelles were: brush borders (1.20), lysosomes (1.20), peroxisomes (1.19), mitochondria (1.17) and basal-lateral membranes (1.13). The values were not significantly different in the ileum. The activities of brush-border enzymes, soluble and mitochondrial malate dehydrogenase, soluble and membrane-associated lactate dehydrogenase and particulate protein content, however, were greater in the jejunal than the ileal enterocytes. 3. Detergent exposed latent alkaline phosphatase activity in jejunal enterocytes and indicated that this enzyme is present not only in the brush border but also in the basal-lateral membrane and soluble fractions of the cell. 4. Isolated jejunal brush-border preprations showed latent activities of both alkaline phosphatase and gamma-glutamyltransferase whereas the activities of alpha-glucosidase and leucyl-beta-naphylamidase were not affected by detergent. Mechanical disruption of these preparations suggested the presence of two forms of alkaline phosphatase in the brush border and provides a technique to assess membrane fragility.
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PMID:Analytical subcellular fractionation studies on enterocytes from the jejunum and ileum of the rat and some properties of brush-border alkaline phosphatase. 2 95

Portions of closed jejunal biopsies from the dog were homogenised and their organelles separated by isopycnic centrifugation on continuous sucrose density gradients. The distributions of marker enzymes for the principal organelles were determined using highly sensitive assay procedures. The following organelles, with assayed marker enzymes and modal densities between brackets were characterised: peroxisomes (catalase, 1.21); brush borders (zinc-resistant alpha-glucosidase, leucyl-beta-naphthyl-amidase, gamma-glutamyl transferase, alkaline phosphatase, 1.20); lysosomes (N-acetyl-beta-glucosaminidase, alpha-mannosidase, 1.19); mitochondria (malate dehydrogenase, 1.18); endoplasmic reticulum (Tris-resistant alpha-glucosidase, 1.16); basal-lateral membranes (5'-nucleotidase, 1.11) and cytosol (lactate dehydrogenase). Homogenisation in isotonic sucrose containing digitonin (0.12 mmol/litre) selectively disrupted lysosomes and increased the equilibrium density of brush border and basal-lateral membranes. This procedure will be used to study the subcellular pathology of naturally occurring intestinal disease in the dog.
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PMID:Subcellular fractionation studies on peroral jejunal biopsies from the dog. 3 Jan 25

The urinary excretion of lactate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase, beta-glucuronidase, and leucine arylamidase was studied in 68 patients with biopsy-proved glomerular, 54 with interstitial renal disease and in 97 patients suffering from primary hypertension. The enzyme output of these 219 patients was compared to that of a reference population of 100 thoroughly selected healthy subjects. The highest incidence of elevated enzyme excretion was observed for N-acetyl-beta-glucosaminidase with 88% in glomerulopathies and 78% in interstitial disease, followed by beta-galactosidase. 94% of the patients with glomerular kidney disease, 90% of those with interstitial disease and about 60% of the subjects with primary benign hypertension revealed an output of at least one enzyme above upper reference limit. The highest average enzymuria occured in glomerulopathies, particularly high values in patients with the nephrotic syndrome. Application of discriminant analysis to the urinary enzyme pattern of glomerular and interstitial renal diseases resulted in an overall correct classification into the appropriate group of 89% of all patients. The discrimination between glomerular and interstitial disease was better in patients with normal renal function than in those with reduced function. Results show, that the analysis of urinary enzyme patterns may be a helpful adjunct for differential diagnosis of kidney diseases.
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PMID:Evaluation of urinary enzyme patterns in patients with kidney diseases and primary benign hypertension. 3 57

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

Acid phosphatase and beta-glucosidase were shown to be present in five species of Ochromonas grown in organic media (O. danica, O. malhanesis, O. munuta, O. sociabilis and Ochromonas sp. 933/4). Acid phosphatase was found to have a pH optimum at 4.0 in O. danica, and at 5.1 in the four other species. No alkaline phosphatase was found in any of the above mentioned species. Beta-glucosidase in the species studied has a pH optimum at 4.6. Low alpha-glucosidase activity was found only in O. danica. Acid phosphatase in all the five species shows an increase in activity during the logarithmic phase of growth and a decrease during the early stationary phase. Beta-glucosidase shows a similar behavior only in O. danica.
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PMID:Comparative study on hydrolases in five species of Ochromonas (chrysomonadina). 23 61

The activities of several enzymes in urine are masked by the presence of interfering substances in native urine. From several methods proposed for the removal of low molecular mass interferences dilution, dialysis, gel filtration, and ultrafiltration have been successfully applied. Gel filtration seems to be of these most suitable. I is effective, accurate, precise and economical. Scale-down procedures provide for acceptable speed. By this method the complete separation of lactate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase, beta-glucuronidase and leucine arylamidase from low molecular mass substances, e.g. a heat-stable, competitive inhibitor of N-acetyl-beta-glucosaminidase was possible. The preparation and determination of urinary enzymes should be thoroughly standardized and controlled. Acceptable precision (coefficient of variation less than 10% between-day) can be achieved with manual spectrophotometric methods.
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PMID:Preparation of urine for enzyme determinations by gel filtration. 44 74


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