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:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzymatic synthesis of lysophosphatidic acid, phosphatidic acid, monoacylglycerol and diacylglycerol from sn-[14C]glycerol 3-phosphate occurs in purified chloroplasts. The results indicate that: (1) the chloroplast extract contains a soluble acylase (acyl-CoA: sn-glycerol 3-phosphate acyltransferase); (2) the envelope fraction contains an acyl-CoA synthetase, a bound acylase (acyl-CoA: acyl-sn glycerol 3-phosphate acyltransferase) and a phosphatidic acid phosphatase; without chloroplast extract in the incubation medium, the envelope is unable to incorporate sn-glycerol 3-phosphate into phosphatidic acid and diacylglycerol; addition of chloroplast extract to the incubation medium induced a fast increase of the incorporation of sn-glycerol 3-phosphate into phosphatidic acid and diacylglycerol; thylakoids being unable to incorporate sn-glycerol 3-phosphate (in presence or absence of soluble chloroplast extract in the incubation medium) our results indicate that the envelope of spinach chloroplast is the site of phosphatidic acid and diacylglycerol synthesis; (3) diacylglycerol actively synthesized by the envelope is also the substrate for the first galactosylation enzyme.
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PMID:Site of synthesis of phosphatidic acid and diacyglycerol in spinach chloroplasts. 83 58

This communication presents the results obtained in tubular aggregates of 24 enzyme histochemical techniques for demonstrating activity of oxidoreductases, transferases, hydrolases and isomerases. The activity characteristics of the tubular aggregates in m. gluteus medius of 18 patients with diseases of the neuromuscular system were almost identical. A high activity of the mitochondrial enzymes, NADPH: tetrazolium oxidoreductase, NADH:tetrazolium oxidoreductase and cytochrome c oxidase, could be shown in the pathological structures, whereas the activity of the mitochondrial enzymes, glycerol-3-phosphate:menadione oxidoreductase, succinate:PMS oxidoreductase, malate:NAD+ oxidoreductase and isocitrate:NAD+ oxidoreductase, and the partial mitochondrial enzymes, malate:NADP+ oxidoreductase and isocitrate:NADP+ oxidoreductase, was very slight or even absent. There was a moderate to strong activity of the glycolytic enzymes lactate:NAD+ oxidoreductase, glyceraldehyde-3-phosphate:NAD+ oxidoreductase, phosphofructokinase, phosphoglucomutase and glucose phosphate isomerase. In contrast, the activity of alpha-glucan phosphorylase was slight. The activity of phosphogluconate:NADP+ oxidoreductase, glucose-6-phosphate:NADP+ oxidoreductase and 5'-nucleotidase was slight, whereas there was no activity of myosin ATPase and mitochondrial ATPase, acid phosphatase or alkaline phosphatase. The high activity of AMP-deaminase was very striking. The activity of peroxidase was moderate. Results obtained with adsorption studies point to adsorption of some of the enzymes studied to the tubular aggregates in vivo and this phenomenon very probably determined the histochemical characteristics of these structures.
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PMID:Histochemical features of tubular aggregates in diseased human skeletal muscle fibres. 317 98

The levels of pancreatic digestive enzymes, lysosomal hydrolases, and protease inhibitors were evaluated in ascites fluid from 24 patients with acute pancreatitis diagnosed as alcoholic, gallstone-induced, or idiopathic. In this group the concentrations of amylase (354 +/- 98 ng/ml), immunoreactive cationic trypsinogen (1840 +/- 238 ng/ml), and immunoreactive elastase 2 (1492 +/- 262 ng/ml) were greatly elevated in comparison to the corresponding serum values. Enzyme levels in ascites from the idiopathic pancreatitis group tended to be higher than the levels from the other two groups. Activity of acid phosphatase and beta-glucuronidase was significantly higher in ascites compared to serum in all groups. On the other hand, levels of immunoreactive alpha 1-protease inhibitor and alpha 2-macroglobulin in ascites fluid were about half the average concentrations reported for normal serum. Significant amounts of tryptic amidase activity (61.7 +/- 13.7 micrograms/ml) were observed, indicating a trypsin-alpha 2-macroglobulin complex. These data indicate an imbalance in the protease-to-inhibitor ratio in ascites fluid from patients with acute pancreatitis. Coupled with elevated ribonuclease activity (27.4 +/- 3.4 units), a positive methemalbumin test in 23 of 24 patients (1.1 +/- 0.4 mg hematin/100 ml), and an average protein concentration of 4.0 +/- 0.2 g/100 ml, these observations demonstrate that abdominal paracentesis and the biochemical analyses of ascites fluid provide useful information related to the biochemical events in acute pancreatitis and may be useful in the diagnosis of difficult cases, but their predictive value of severity remains to be established.
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PMID:Biochemical studies in peritoneal fluid from patients with acute pancreatitis. Relationship to etiology. 381 84

A patient with Ph1-positive chronic myeloid leukaemia (CML) presented in extramedullary blast crisis. Whereas the peripheral blood and bone marrow features were consistent with the chronic phase of CML, study of the enlarged lymph nodes demonstrated massive replacement by Ph1-positive blast cells of lymphoblastic morphology. Such blast cells showed diffuse acid phosphatase positivity, were positive for TdT, and had an enzyme pattern (adenosin-deaminase, purine-nucleosidephosphorilase and lactate-dehydrogenase) typical of immature T-cells. To further characterize the phenotype of the blast cells, they were analyzed for surface markers using a panel of monoclonal antibodies selected to identify differentiation antigens of T cells, B cells and myeloid cells. The results of the latter analysis were consistent with an early T-cell origin of the blast cells, since they were positive for TdT, CRIS1 (T1), E rosettes and OKT10, and were negative for OKT3, Leu3 and OKT8. These features demonstrate that T-cell markers may also be expressed in blast crisis of CML and provide evidence that T-cells may share a common stem cell with myeloid and B-cells in CML.
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PMID:Early T-cell features in blast crisis of Ph1-positive chronic myeloid leukaemia. 393 Dec 8

1. Homogenates of the mucosa of the small intestine of the guinea pig were separated by fractional sedimentation into seven different fractions. The enzymic properties of some of these subcellular fractions were compared with those obtained from the mucosa of the small intestine of the rabbit and cat. 2. The enzymic properties of the low-speed sediment (15000g-min.) were investigated and it was shown that invertase and alkaline ribonuclease were predominantly located in this subcellular fraction, whereas alkaline phosphatase, aryl-amidase, acid phosphatase, acid ribonuclease and phosphoprotein phosphatase, though true constituents of this fraction, occurred to varying degrees in other subcellular structures also. 3. It was shown that the most probable source of the enzymic activities observed in the low-speed sediment was the brush border. Electron micrographs of the purified brush-border fraction indicated vesicles derived from the brush-border membrane. 4. A method is described for the fractionation of mucosal homogenates into a brush border-plus-nuclei fraction, a mitochondrial fraction, a microsomal fraction and a particle-free supernatant. The fractions were shown to be relatively pure, as indicated by the distribution of invertase, DNA, succinate dehydrogenase, glucose 6-phosphatase and 6-phosphogluconate dehydrogenase. 5. Most of the activity of four lysosomal enzymes present in the nuclei-free homogenate was sedimented at 375000g-min., suggesting the occurrence of lysosomal particles in mucosal homogenates. 6. Further fractionation of the microsomal membranes into three fractions is described. The enzymic composition of the membrane fractions is given and discussed in relation to their structure as seen in electron micrographs.
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PMID:Studies on the fractionation of mucosal homogenates from the small intestine. 428 74

The present study was made to isolate and assess some physiological characteristics of root nodule-colonizing fungi. During this study, 17 fungal species were isolated from root nodule samples taken from faba bean plants (Vicia faba L.) collected from different sites at Assiut area (Egypt). The growth of faba bean plants in pots was significantly promoted by soil inoculation with most fungi. Growth was checked in pots with inocula of Cladosporium cladosporioides, Fusarium moniliforme, F: oxysporium, F solani, Macrophominia phaseolina and Rhizoctonia solani which were added separately. All growth-promoting fungi were capable of producing cellulase, pectin lyase, polygalacturonase, protease, urease, amidase, acid phosphatase, alkaline phosphatase and arylsulfatase in growth medium supplemented with the corresponding substrates. Four fungal species, Aspergillus awamori, A. flavus, Penicillium chrysogenum and Trichoderma koningii showed the highest rates of enzyme formation. The effect of the addition of six trace elements to the growth media at 30 micromol/ml on enzyme production revealed some dependency on species, enzyme and metal ion. Cd2+, Hg2+ and Zn2+ generally inhibited enzyme activity. Cu(1+), Fe3+ and Al3+ showed a stimulatory effect. Fungicides (afugan and tilt) and herbicides (brominal and fusilade) at 50 ppm generally promoted enzyme activity, but insecticides (kelthane and fenvalerate) caused some inhibition to enzyme activities. Salinization of the growth media with NaCl strongly inhibited the enzymatic activity of all fungi at concentrations between 0.5 and 1.5%.
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PMID:Physiological aspects of fungi isolated from root nodules of faba bean (Vicia faba L.). 1077 56

OBJECTIVE: To test a new system for the biotyping of Streptococcus mutans, based on the measurement of enzyme activity, and to investigate the relationship between biotype and in vitro susceptibility to seven clinically useful antibiotics. METHODS: In total, 160 oral isolates of S. mutans were classified into different biotypes with the APIZYM test for enzyme activity, excluding results that were positive or negative in >80% of the strains. The susceptibility of all 160 strains to amoxycillin, cefazolin, erythromycin, clindamycin, vancomycin, teicoplanin and imipenem was tested by dilution in a solid medium. Statistical analysis of susceptibility (mean minimum inhibitory concentrations (MICs)) was based on chi-squared tests. RESULTS: Eight different biotypes (1-8) were identified on the basis of three kinds of enzyme activity: valine aryl amidase, acid phosphatase and alpha-galactosidase. Biotype 5 was found to be the most common. The mean MIC values showed strains belonging to biotype 4 to be the most susceptible to amoxycillin, cefazolin and erythromycin, whereas biotype 1 was the least susceptible to teicoplanin. CONCLUSIONS: The proposed biotyping method, which is relatively fast and simple to perform, provided reproducible results, and may contribute to clinically effective treatment of S. mutans infections.
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PMID:A new biotyping method for Streptococcus mutans with the API ZYM system. 1185 23

The cricopharyngeal muscle (CPM) is essential for normal deglutition. Pharyngeal dysphagia commonly results from impaired or uncoordinated CPM dilation. Dysfunction of the CPM has also been implicated in the genesis of Zenker's (pharyngoesophageal) diverticulum. Despite the CPM's significance, little is understood about its morphology. We studied CPM biopsy specimens from 20 patients with Zenker's diverticulum and from 5 fresh cadaver patients with detailed histologic techniques to include fiber size and shape and adenosine triphosphatase, reduced nicotinamide adenine dinucleotide, trichrome, succinate dehydrogenase, cytochrome C oxidase, periodic acid-Schiff reaction, oil red O, acid phosphatase, Congo red, crystal violet, and monoadenylate deaminase stains. The normal CPM has unique morphological characteristics, with some myofibers having staining properties that are a hybrid between striated muscle and muscle spindle. The variable orientation of the muscle fibers is also different from that of most other striated musculature. Of the 20 Zenker CPM specimens, 4 specimens did not reveal any significant differences from controls (2 of which had insufficient amounts of tissue for complete analysis). In the remaining 16 specimens, several abnormalities existed, including excessive size variation (16/16), grouping of atrophic fibers (9/16), target or targetoid formations (4/16), cores (2/16), and ragged red fibers (2/16). The final pathological pattern of the 16 specimens was neurogenic in 7, myopathic in 4, and mixed (with neurogenic predominance) in the remaining 5. Two specimens contained significant lymphocytic inflammatory infiltrates. We conclude that the unique neuromuscular function of the CPM in deglutition is likely due to its fiber orientation and the hybrid nature of some of the myofibers. Morphological disturbances of the CPM impair its dilation and may account for the development of Zenker's diverticulum. This disturbance is most often due to progressive denervation of the CPM.
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PMID:Morphology of the cricopharyngeal muscle in Zenker and control specimens. 1212 11

Extracts of Aspergillus niger NRRL3 catalyzed dephosphorylation of AMP, GMP, CMP and UMP over a wide range of pH values from pH 1.5 to pH 10. They also catalyzed hydrolytic deamination of only cytidine out of the tested ribonucleotides, ribonucleosides and bases. Neither cleavage of the N-glycosidic linkages of these nucleotides nor those of the corresponding nucleosides could be effected by the extracts. Phosphate liberation from the four RNA monomers seemed to be effected by two phosphate-non repressible phosphatases, acid and alkaline. Optimum activity of the acid phosphatase with all the substrates was at pH2 and 40 degrees C while that of the alkaline phosphatase was at pH8 and 40 degrees-70 degrees C. Affinities of both phosphatases for the different ribonucleotides were in the order of magnitude AMP, CMP and phph > GMP > UMP. Freezing and thawing of the extracts had no effect either on the activities of two phosphatases or on that of the aminohydrolase. However, heating the extracts at 55 degrees for 25 min, in absence of the substrate, inactivated the phosphatases and had no effect on the deaminase. No evidence for the involvement of specific nucleotidases in ribonucleotides dephosphorylation was recorded.
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PMID:Hydrolysis of RNA monomers by extracts of Aspergillus niger NRRL3. 1518 88

Kalmia angustifolia is an ericaceous shrub that can rapidly spread on recently harvested boreal forest sites, causing a slow-down in soil nutrient cycling and reduced growth of spruce seedlings. It has been hypothesized that tannins released from Kalmia litter suppress soil enzyme activity, and are thus important in controlling ecosystem structure and processes. Here the effects of different concentrations of tannins extracted from both Kalmia and black spruce (Picea mariana) foliage were tested on enzyme activities of soil extracts. Then the effects of various Kalmia-black spruce litter mixtures on soil enzyme activity were investigated. Lastly, the correlation between Kalmia cover in the field and soil enzyme activity was measured. Both tannin types suppressed beta-glucosidase and acid phosphatase activities, and the magnitude of these effects was concentration-dependent. beta-glucosidase and amidase activity decreased linearly with an increasing Kalmia : spruce litter ratio added to soil. A field survey of 24 sites revealed a negative relationship between percentage Kalmia cover and beta-glucosidase activity. Collectively, results of the three experiments converge to support the claim that enzyme inhibition by litter tannins has evolved as an important mechanism controlling ecosystem processes and structure following Kalmia invasion on recently disturbed forest sites.
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PMID:Soil enzyme inhibition by condensed litter tannins may drive ecosystem structure and processes: the case of Kalmia angustifolia. 1763 28


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