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:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Liver homogenates have been submitted to quantitative fractionation by differential centrifugation. Three particulate fractions: N (nuclear), ML (large granules), and P (microsomes), and a final supernate (S) have been obtained. The biochemical composition of the microsomal fraction has been established from the assay and distribution pattern of 25 enzymatic and chemical constituents. These included marker enzymes for mitochondria (cytochrome oxidase), lysosomes (acid phosphatase and N-acetyl-beta-glucosaminidase), and peroxisomes (catalase). The microsomal preparations were characterized by a moderate contamination with large cytoplasmic granules (only 6.2% of microsomal protein) and by a high yield in microsomal components. Enzymes such as glucose 6-phosphatase, nucleoside diphosphatase, esterase, glucuronyltransferase, NADPH cytochrome c reductase, aminopyrine demethylase, and galactosyltransferase were recovered in the microsomes to the extent of 70% or more. Another typical behavior was shown by 5'-nucleotidase, alkaline phosphatase, alkaline phosphodiesterase I, and cholesterol, which exhibited a "nucleomicrosomal" distribution. Other complex distributions were obtained for several constituents recovered in significant amount in the microsomes and in the ML or in the S fraction.
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PMID:Analytical study of microsomes and isolated subcellular membranes from rat liver. II. Preparation and composition of the microsomal fraction. 415 Apr 89

1. A collagenase digest of rat kidney cortex was separated into four bands by zonal centrifugation. 2. Two of these bands were shown by light-microscopy to contain glomeruli and tubular fragments, which were free from each other and well separated from other renal material. 3. Protein, N-acetyl-beta-glucosaminidase, 5'-nucleotidase, l-leucine beta-naphthylamidase, leucine aminopeptidase, acid phosphatase and alkaline phosphatase were assayed across the gradient. 4. The greater proportion of these enzyme activities was recovered in the tubular fragments and acid phosphatase was the only enzyme detected in significant amounts in the glomeruli. 5. Tubular fragments and glomeruli were sedimented and multiple forms of beta-naphthylamidase, N-acetyl-beta-glucosaminidase, acid phosphatase and alkaline phosphatase were investigated by starch-gel electrophoresis.
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PMID:The distribution of some hydrolases in glomeruli and tubular fragments prepared from rat kidney by zonal centrifugation. 433 86

Human jejunal biopsy slices were maintained in culture for up to 48 hours. At 24 hours there was good morphological preservation but by 48 hours there was ultrastructural evidence of damage to the enterocytes. During culture the tissue had lost a certain amount of protein. At the same time the levels of three brush border enzymes (alkaline phosphatase, alpha-glucosidase, and leucyl-beta-naphthylamidase) and one lysosomal enzyme (N-acetyl-beta-glucosaminidase) showed a progressive decrease. Alkaline phosphatase, alpha-glucosidase, and N-acetyl-beta-glucosaminidase accumulated in the medium throughout the experimental period to give a medium:tissue distribution ratio of between 2 and 9. Leucyl-beta-naphthylamidase had a medium:tissue ratio of 140 after 48 hours of culture suggesting a selective secretion of this enzyme by the tissue.
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PMID:Enzyme changes in human small bowel mucosa during culture in vitro. 443 22

Effects of the dopamine agonist 2-bromo-alpha-ergocryptine (bromocriptine) on plasma and pituitary PRL and enzyme activities in lactating and postlactating rats have been investigated. Lactating rats which had been suckling their young for 3 days were given a single sc injection of bromocriptine or solvent. The treated and control animals were divided into 2 further groups. One group (lactating rats) was permitted to suckle their pups for a further 12 or 24 h; the young were removed from the other group (postlactating rats). Homogenates were prepared from the anterior pituitaries and assayed for organelle marker enzyme activities. When 0.5-500 micrograms bromocriptine were administered to lactating rats for 24 h, pituitary PRL was increased by all doses, but only the 500-micrograms dose significantly reduced plasma PRL. Total protein was unchanged, lysosomal acid PRL proteolytic activity increased 8-fold, N-acetyl-beta-glucosaminidase and beta-glucuronidase (lysosomes) were unchanged, acid phosphatase (lysosomes and endoplasmic reticulum) was increased by three of four doses, 5'-nucleotidase and alkaline phosphatase (plasma membrane) were increased 4-fold, neutral-alpha-glucosidase (endoplasmic reticulum) and malate dehydrogenase (mitochondria) were unchanged, and catalase (peroxisomes) was significantly increased. Bromocriptine (500 micrograms) administration to lactating and postlactating rats for 12 and 24 h significantly decreased the pituitary DNA but not the total protein content of the pituitaries in all animals. The lysosomal acid PRL proteolytic activity and the lysosomal enzyme activities, N-acetyl-beta-glucosaminidase and beta-glucuronidase, were increased by suckling withdrawal alone. Acid PRL proteolytic activity was further increased (to 18-fold) by coadministration of bromocriptine, whereas the increase in the activities of the other lysosomal marker enzymes was blocked. Malate dehydrogenase activity (mitochondria) was also increased by litter removal and blocked by bromocriptine. The activity of the plasma membrane markers 5'-nucleotidase and alkaline phosphatase were increased by litter removal, and bromocriptine further increased both enzyme activities. The activity of neutral-alpha-glucosidase (endoplasmic reticulum) was unchanged by any treatment. The results demonstrate that bromocriptine produces significant changes in the activities of lysosomal marker enzymes, particularly acid PRL proteolytic activity, as well as marker enzymes of plasma membranes and other organelles in pituitaries of lactating and postlactating rats.
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PMID:Effects of bromocriptine on pituitary organelle marker enzyme activities in lactating and postlactating rats: selective activation of lysosomal prolactin proteolytic activity. 608 93

The influence of two surface-active food additives on the integrity and permeability of rat ileal mucosa has been studied. We determined the activity of N-acetyl-beta-glucosaminidase, a lysosomal enzyme, in the rat intestinal lumen after deposition of polyoxyethylene (20) sorbitan monostearate (polysorbate 60; Tween 60) or polyoxyethylene (20) sorbitan monooleate (polysorbate 80; Tween 80) in a section of ligated, cannulated gut. We also determined the activities of N-acetyl-beta-glucosaminidase, alkaline phosphatase, 5'-nucleotidase and phospholipase A2 in mixtures of isolated mucosal cells and polysorbate 60 or polysorbate 80. The activity of N-acetyl-beta-glucosaminidase was increased in the luminal contents of the cannulated gut 15 min after deposition of either polysorbate 60 or polysorbate 80 (10 mg/ml fluid instilled into gut). It was also increased in mixtures of mucosal cells and polysorbate 60 or polysorbate 80 (0.1-10 mg/ml). In contrast, the activities of alkaline phosphatase and 5'-nucleotidase were unaffected and that of phospholipase A2 was decreased by the presence of either polysorbate. These findings indicated that polysorbate 60 and polysorbate 80 released lysosomal enzymes from the intestinal mucosal cells and that these agents might damage the intestinal mucosa and increase its permeability. We therefore determined the intestinal permeability to sodium fluorescein in the absence and presence of polysorbate 60 or 80 and found that the permeability was slightly increased in the presence of either of the compounds at concentrations of 10 mg/ml fluid instilled into gut. It is possible therefore that surface-active food additives might impair the function of the mucosal barrier and increase the permeability of the gut to potentially toxic and pathogenic molecules.
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PMID:Influence of surface-active food additives on the integrity and permeability of rat intestinal mucosa. 609 20

We determined the urinary excretion of the enzymes aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), gamma-glutamyltransferase (EC 2.3.2.2), and N-acetyl-beta-glucosaminidase (EC 3.2.1.30) in two groups of renal-transplant recipients at different times after transplantation (1.8 months and 52 months, respectively). Both groups of patients showed a higher rate of enzyme excretion than did a reference group of healthy persons. More aminopeptidase and N-acetyl-beta-glucosaminidase were excreted during the early period after transplantation than later. The time-dependence of urinary enzyme excretion was confirmed in six renal-transplant recipients studied during the course of 15 months after transplantation. There was a general correlation between the extent of urinary enzyme excretion and both the time after transplantation and the daily dose of prednisolone. Therefore, it is necessary to take into account this influence on the extent of urinary enzyme in renal-transplant recipients if urinary enzyme excretion is used as an indicator of renal disorder and especially as an early predictor of transplant rejection.
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PMID:Urinary enzyme excretion by renal-transplant recipients in relation to interval after transplantation. 612 28

The activity of the marker enzymes lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, gamma-glutamyl transferase, leucyl-beta-naphthylamidase (brush border); 5-nucleotidase (basolateral membrane); and acid phosphatase and N-acetyl-beta-glucosaminidase (lysosomes) in jejunal biopsies from patients with the stagnant-loop syndrome and controls was studied. The activity of gamma-glutamyl transferase was increased in the patient group; the activity of the other enzymes did not differ significantly in patients and controls. The DNA to protein ratio was increased in the patient group. The results do not support the hypothesis of epithelial damage in the human stagnant-loop syndrome.
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PMID:Enzymatic activities in jejunal biopsy specimens from patients with the stagnant-loop syndrome. 614 77

Human lymphocytes were isolated from defibrinated blood by Ficoll-Hypaque centrifugation with erythrocyte hypotonic lysis. Homogenates of mixed lymphocytes were subjected to analytical subcellular fractionation by sucrose gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their marker enzymes: cytosol (lactate dehydrogenase), plasma membrane (5'-nucleotidase), endoplasmic reticulum (neutral alpha-glucosidase), mitochondria (malate dehydrogenase), lysosomes (N-acetyl-beta-glucosaminidase), peroxisomes (catalase). gamma-Glutamyl transferase was exclusively localized to the plasma membrane. Leucine amino-peptidase, especially when assayed in the presence of Co2+, was also partially localized to the plasma membrane. Experiments with diazotized sulphanilic acid, a non-permeant enzyme inhibitor, showed that these plasma membrane enzymes are present on the cell surface. No detectable alkaline phosphatase was found in the lymphocytes. Acid phosphatase and beta-glucuronidase were localized to lysosomes and there was some evidence for lysosomal heterogeneity. Leucine amino peptidase, optimal at pH 8.0, showed a partial localization to intracellular vesicles, possibly lysosomes, especially when assayed in the presence of EDTA. These studies provide a technique for determining the intracellular distribution of hitherto unassigned lymphocyte constituents and serve as a basis for investigating the cell pathology of lymphocytic disorders.
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PMID:Enzyme analysis and subcellular fractionation of human peripheral blood lymphocytes with special reference to the localization of putative plasma membrane enzymes. 614 55

In 25 patients (10 women and 15 men) aged 37 to 68 years activity of the following enzymes has been determined by the use of semiquantitative cytochemical methods: acid and alkaline phosphatase, beta-glucuronidase, N-acetyl-beta-glucosaminidase and myeloperoxidase. Additionally the content of glycogen and lipids has been determined in the cells studied. An increase of the myeloperoxidase and acid phosphatase activity and a decrease of the glycogen and the lipid content has been stated in neutrophils of the patients. Above alterations may reflect antitumor reactivity of neutrophils or nonspecific neutrophil response against inflammatory changes accompanying the tumor area.
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PMID:Enzymes of peripheral blood neutrophils in patients with cancer of the stomach. 631 12

The present study was designed to find useful markers for detection of renal damage due to gentamicin (GM). Following the administration of 80 mg/kg GM, there were significant increases in urinary protein contents and alkaline phosphatase, N-acetyl-beta-glucosaminidase, lactate dehydrogenase, gamma-glutamyl transpeptidase and lysozyme activities. Alterations of these parameters had a peak at the 7th or 10th day and values restored to near normal levels by the 15th day. Light microscopic observations of the kidney on the 10th day showed mainly the necrosis of proximal tubular epithelial cells in the renal outer cortex, and there was regeneration of epithelial cells on the 15th day. In addition, when 1 mg/kg HgCl2 was given to rats, there were increases in urinary enzyme activities and protein contents, and BUN. The kidney of rats that received HgCl2 showed the necrosis of tubular epithelial cells in the renal inner cortex. It is considered from these results that determination of the activities of various urinary enzymes may be useful markers to detect tubular damage induced by GM.
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PMID:[Studies on the nephrotoxicity of aminoglycoside antibiotics and protection from these effects. (1). Nephrotoxicity of gentamicin and mercuric chloride]. 651 81


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