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)

We isolated 15 mutants of Pseudomonas aeruginosa PAO which were defective in the formation of certain extracellular proteins, such as elastase, staphylolytic enzyme, and lipase ( Xcp mutants). The mutations were mapped on the chromosome by conjugation and transduction. The locations were xcp -1 near 0', with the gene order cys-59- xcp -1- proB , and loci xcp -2, xcp -3, and xcp -31 at 35', with the gene order trpC , D- xcp -3/ xcp -31- xcp -2- argC . Loci xcp -4 and xcp -41 through xcp -44 were cotransducible with proA at 40'; loci xcp -5, xcp -51, xcp -52, and xcp53 were located at 55', with the gene order leu-10- trpF -met-9010- xcp -53- xcp -5/ xcp -51/ xcp+ ++-52, and xcp -6 was located at 65' to 70', between catA and mtu-9002. Nine mutations ( xcp -2, xcp -3, xcp -31, xcp -4, and xcp -41 through xcp -45) caused decreased production of extracellular enzymes. Six strains with mutations xcp -1, xcp -5, xcp -51, xcp -52, xcp -53, and xcp -6 produced cell-bound exoproteins and had defective release mechanisms. The regulation of production of alkaline phosphatase and phospholipase C is different from other exoproteins , such as elastase, but they all seem to share a common release mechanism. Alkaline protease had separate mechanisms for regulation and release, since this protease was found in culture supernatants of all but one of the mutants, and none of the strains had cell-bound enzyme.
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PMID:Genetic mapping and characterization of Pseudomonas aeruginosa mutants defective in the formation of extracellular proteins. 642 94

Twelve whole mite extracts (WME) from seven sources were examined for their content of the allergen Dpt 12, protein content, and the inhibitory capacity in RAST by use of paper discs coupled with either WME or Dpt 12. Linear regression analysis demonstrated that the concentration of Dpt 12 determined either by single radial immunodiffusion or by RAST inhibition did not correlate with either the RAST-inhibition titer with use of discs coupled with WME or with protein content, suggesting that Dpt 12 content does not reflect the overall potency of WMEs. However, statistically significant correlations were obtained between Dpt 12 content and whole mite-RAST inhibition titers if extracts from the same manufacturer were examined or if data obtained from extracts containing large Dpt 12 to protein concentrations (greater than 25%) were excluded from the analysis. In contrast, statistically significant correlations between protein concentration and WME-RAST inhibition titers (p = 0.00037) and between Dpt 12 content and Dpt 12 RAST-inhibition titers (p = 0.00001) were found. Thermal stability studies demonstrated that Dpt 12 per se and WMEs were stable at 4 degrees C for up to 3 mo. Storage at 23 degrees C for 3 mo, however, resulted in partial loss of both Dpt 12 and whole-mite activity. Substantial losses occurred at 36 degrees C for both 1-month and 3-month incubation periods. Esterase, esterase lipase, and alkaline phosphatase were found in three WMEs studied. Dpt 12 was biochemically unrelated to these enzymes.
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PMID:Quantitation and thermal stability of the mite allergen DPT 12 in whole mite extracts. 643 11

A pancreas-specific antigen was identified by immunologic techniques and purified from saline extract of human pancreas. The purified pancreas-specific antigen was shown to be homogeneous by polyacrylamide gel electrophoresis under both denaturing and non-denaturing conditions. It had a molecular weight of 44000 as estimated by gel filtration or sodium dodecyl sulfate-gel electrophoresis, and a sedimentation coefficient of 3.4 S as analyzed by sucrose gradient centrifugation. Pancreas-specific antigen possessed an isoelectric point of 4.9 and migrated to alpha-beta region upon immunoelectrophoresis. By colorimetric assay procedures, pancreas-specific antigen exhibited no enzyme activity, such as amylase, protease, esterase, lipase, acid phosphatase, alkaline phosphatase peroxidase, deoxyribonuclease or ribonuclease. Immunoreactivity of pancreas-specific antigen was sensitive to proteolytic enzymes, perchloric acid and high temperature (70 degrees C, 10 min); but insensitive to neuraminidase or beta-glucosidase. Immunohistochemical staining revealed that pancreas-specific antigen was located in acinar cells of human pancreas. In addition, a higher concentration of pancreas-specific antigen was detected in pancreatic juice than in the saline extract of pancreas. This newly identified pancreas-specific antigen, therefore, may be a useful marker protein in physiological studies of pancreas and pancreatic secretion.
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PMID:Purification and characterization of a human pancreas-specific antigen. 678 69

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

Some hydrolytic enzyme activities, mainly typical of lysosomal localization, have been determined in blood sera from patients who ingested a rapeseed oil (denatured with anilines and treated by a thermal process), and in healthy subjects. beta-N-Acetylglucosaminidase, beta-D-glucosidase, beta-D-glucuronidase, alpha-L-fucosidase and leucine aminopeptidase activities were significantly higher when compared with controls (p less than 0.001); higher activities but not significant (p less than 0.2) differences were found for alpha-D-mannosidase and alkaline phosphatase. In contrast, beta-D-galactosidase, alpha-D-galactosidase, acid phosphatase and lipase showed lower activities than controls. The significance of these results is discussed.
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PMID:Hydrolytic enzyme activities, mainly from lysosomal localization, in sera from patients who ingested a toxic oil. 683 4

Heparin-independent release of lipoprotein lipase activity from isolated perfused rat hearts was measured and related to the rapid turnover of the enzyme. Hearts consistently released lipoprotein lipase activity (2.1 +/- 0.2 U/g released per min) during 60 min of nonrecirculating perfusion without heparin. This rate of release did not significantly differ from that measured in heparin-perfused hearts after the first 10 min of perfusion (2.2 +/- 0.2 U/g released per min). The fractional release rate of lipoprotein lipase activity during nonheparin perfusion was 1.3% per min, which was higher than that calculated for alkaline phosphatase (0.002%) and creatine kinase (0.03%) activities. The lipase activity released was activated 4-fold by serum and inhibited 94 and 88% by 0.5 M NaCl and 3 mg/ml protamine sulfate, respectively. Lipoprotein lipase activity in the 1-min heparin-releasable (extracellular) and residual (intracellular) compartment remained stable during the last 40 min of nonheparin perfusion. During this period total heart, intracellular and extracellular enzyme t1/2 were calculated to be 52, 42 and 10 min, respectively. The results are consistent with the postulate that continuous release of lipoprotein lipase into the vascular compartment may be an important determinant of its rapid turnover in the heart, and possibly other tissues.
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PMID:Heparin-independent release of lipoprotein lipase activity from perfused rat hearts. 688 86

Mercury is known to modify enzyme activity through oxidation of thiol groups and respective reverse reactions in vitro and in vivo. However, variations in the activity of carbohydrates, and the significance of this variation after mercury poisoning in different species, has not been established. In the present report, the effects of inorganic mercury on selected hepatic enzymes was studied in the freshwater fish Channa punctatus. Quantitative data clearly showed a dose-response relationship between the amount of mercury retained in the liver and inhibition of enzymes (i.e. alkaline phosphatase, glucose-6-phosphatase, amylase, maltase, lactase, lipase and dehydrogenases). Mechanisms and significance of their modification have also been discussed.
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PMID:Co-enzyme effects of inorganic mercury in the liver of a freshwater fish Channa punctatus. 718 6

Enzymological data on alkaline phosphatase, acid phosphatase, glucose-6-phosphatase, cholinesterase and lipase obtained in the kidney of rats, fed on molybdenum (Mo) and copper (Cu), are reported. Antagonistic or synergistic behaviour has been determined by feeding the rats simultaneously on these two metals. Molybdenum inhibited all other enzymes except acid phosphatase and lipase. Complete inhibition of alkaline phosphatase was recorded after copper treatment. The combined treatment with molybdenum and copper exhibited reversible enzyme changes, however, cholinesterase activity remained inhibited.
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PMID:Effect of molybdenum and copper on key enzymes of rat kidney with special reference to physiological antagonism. 724 24

The numerous physiological and nutritional factors which influence the concentration of serum calcium are considered. The causes of hypercalcaemia and hypocalcaemia are briefly discussed, with particular reference to the clinical symptoms and pathology. The effect of the acid-base status on the serum-ionized calcium level is stressed. The causes of changes in the serum concentrations of phosphorus and magnesium are briefly reviewed, along with the abnormalities of lactate, pyruvate, and hydrogen ion concentrations. The kidney function tests, blood urea nitrogen, serum creatinine, and the renal clearance tests are discussed, with emphasis placed on correlating their results with the findings from repeated urinalyses. The important physiologic influences and pathological processes which result in changes in the concentrations of these parameters are delineated. The causes of increases in the serum enzymes, alkaline phosphatase, alanine transaminase, asparate transaminase, lactic dehydrogenase, sorbitol dehydrogenase, glutamic dehydrogenase, gamma glutamyl transpeptidase, creatinine phosphokinase, amylase and lipase are discussed. The changes in serum bilirubin concentration and its components are fully described, with emphasis placed on the correlation of the findings with urinalysis data and the complexities resulting from the numerous pathologic conditions causing jaundice. These conditions are listed for each of the domestic animals. The other liver function tests, bromosulphthalein dye retention or excretion, serum uric acid and blood ammonia concentration are briefly considered. All the tests described are very useful, and frequently essential, in aiding the veterinary practitioner to arrive at a diagnosis and prognosis, but they never replace clinical acumen.
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PMID:Correlation of changes in blood chemistry with pathological changes in the animal's body: II Electrolytes, kidney function tests, serum enzymes, and liver function tests. 727 79

An experiment was conducted to determine the effect of two early nutrient restriction programs on performance, selected characteristics of the gastrointestinal tract (GIT), and activities of digestive enzymes of broiler chickens. Three hundred and sixty male broiler (Ross x Ross) chicks kept in floor pens were assigned to three groups. The control group (C) was given ad libitum access to feed from 1 to 48 d of age. Another group was restricted from 11 to 14 d (R4) of age to an energy intake of .74 x BW.67 kcal ME/d, and a third group was restricted from 7 to 14 d (R7) of age to an energy intake of 1.5 x BW.67 kcal ME/d. Then, both restricted groups were given ad libitum access to feed through 48 d. Body weight and feed intake were determined weekly and selected carcass characteristics were measured at 48 d of age. Broilers also were sampled at 7, 14, 21, and 42 d of age to obtain data on components of the GIT (proventriculus, gizzard, pancreas, and small intestine) and activities of selected digestive enzymes. Feed-restricted groups were lighter in body weight (P < .01) at 14 and 48 d of age than the C group but were superior in overall feed efficiency. No treatment effects were observed for percentage yields of breast meat and abdominal fat pad. Absolute weights of GIT components were significantly reduced at 14 d of age by feed restriction. However, GIT components increased in weight more quickly after refeeding than did the whole body. Restricted groups had reduced (P < .01) specific activities of jejunal alkaline phosphatase and pancreatic trypsin, amylase, and lipase as compared with the C group at 14 d of age but not at 21 and 42 d of age. Relative activities for jejunal maltase and sucrase were greater (P < .01) at 21 d of age in the R4 and R7 groups than in the C group. The present data show that feed restriction results in transient changes in organs and activities of digestive enzymes, suggesting a functional adaptation to feed restriction.
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PMID:Effect of early nutrient restriction on broiler chickens. 2. Performance and digestive enzyme activities. 750 92


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