Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Gene/Protein
Disease
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Drug
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Compound
Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
Compound
Query: EC:3.1.3.1 (
alkaline phosphatase
)
47,916
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Early distinction between acute alcoholic pancreatitis is important, because of possible emergency endoscopic sphincterotomy in case of biliary pancreatitis. The aim of this study was to evaluate the value of L/A ratio in the diagnosis of acute alcoholic pancreatitis. From 1990 to end 1993, 133 patients with acute pancreatitis were reviewed. Inclusion criteria were: 1) abdominal pain, 2) pathological serum amylase or serum
lipase
on admission or within 24 hours after beginning or abdominal pain, 3) acute pancreatitis at the echography or CT scan within 48 hours after admission. 60 patients met the inclusion criteria (31 alcoholic pancreatitis, 19 biliary pancreatitis and 10 pancreatitis of other causes). L/A ratio was studied in terms of delay from beginning of abdominal pain. There was no statistical difference between alcoholic and biliary pancreatitis at any time of the study, with the exception of admission. AST, ALT and
alkaline phosphatase
were higher in biliary pancreatitis than in alcoholic pancreatitis. AST and ALT were the best biochemical tests to diagnose biliary pancreatitis. Blamey's criteria can also contribute to diagnose biliary pancreatitis. These biochemical tests are the most helpful if they are collected very soon in the evolution of acute pancreatitis. It is concluded that L/A ratio is not helpful in the diagnosis of alcoholic acute pancreatitis.
...
PMID:[Can the L/A ratio identify acute alcoholic pancreatitis?]. 757 83
In Pseudomonas aeruginosa, several exoproteins synthesized with a signal sequence (elastase,
lipase
, phospholipases,
alkaline phosphatase
and exotoxin A) are secreted by a two-step mechanism. They first cross the inner membrane in a signal sequence-dependent way, and are further translocated across the outer membrane in a second step requiring secretion functions encoded by several xcp genes. Ten xcp genes have already been characterized (Bally et al., 1992a). In this study, two additional xcp genes, xcpP and xcpQ, are described. They are located in the 40 min region of the chromosome where they probably define an operon, divergent from the xcpR-Z operon previously characterized in this region. These two genes encode two proteins, XcpP and XcpQ, similar to PulC and PulD of the pul system of Klebsiella oxytoca. Moreover, the two divergent operons share a common regulation which is growth-phase dependent.
...
PMID:Xcp-mediated protein secretion in Pseudomonas aeruginosa: identification of two additional genes and evidence for regulation of xcp gene expression. 793 33
We have examined the effects of administration of the blood substitute, liposome-encapsulated haemoglobin (LEH), in the normovolaemic rat. Test groups included LEH, lyophilized EH, the liposome vehicle, unencapsulated haemoglobin and normal saline, which were injected into the tail vein (n = 6; n = 3 for sham and saline groups). Administration of LEH (2.5 g phospholipid, 1.25 g haemoglobin/kg rat) was followed by blood sampling at 2 h, 24 h, 1 wk and 2 wk. Blood samples were analysed for alanine aminotransferase, aspartate aminotransferase,
alkaline phosphatase
, gamma-glutamyltransferase, total and indirect bilirubin, serum creatinine, albumin, total protein,
lipase
, cholesterol, blood urea nitrogen, haematocrit, haemoglobin and differential white blood cell counts. Observed effects following injection were mild and transient, with baseline values recovered at 1 wk. Alanine aminotransferase increased moderately in the LEH group at 24 h to 601 +/- 143 IU/dl (P < 0.0001), with a return to baseline at 1 wk. Aspartate aminotransferase showed a smaller increase from 46 +/- 5 to 162 +/- 40 at 24 h and also returned to baseline at the 1 wk measurement (P < 0.001). The transient increase in serum transaminases was not observed for the lyophilized LEH group. Tissue sections showed accumulation of liposome groups in resident macrophages of the liver and spleen. Incubation of an adherent population of human peripheral blood monocytes with LEH in culture did not elicit the production of the inflammatory cytokine, tumour necrosis factor. Pre-incubation of monocytes with LEH prior to exposure to endotoxin did, however, result in a reduced expression of this inflammatory cytokine.
...
PMID:Transient changes in the mononuclear phagocyte system following administration of the blood substitute liposome-encapsulated haemoglobin. 798 44
Five enzyme materials (gamma-glutamyltransferase,
alkaline phosphatase
, creatine kinase, alanine aminotransferase and prostatic acid phosphatase) are currently certified using a reference method. Furthermore, feasibility studies have been performed for four other enzymes (aspartate aminotransferase, lactate dehydrogenase, amylase and
lipase
). They indicated that these enzymes can be purified and stabilized, but the materials have not yet been certified. This shows that the most important enzymes in clinical laboratories can be purified, and stabilized, without significant alteration of their catalytic properties. By carefully choosing a matrix, the commutability of these enzyme preparations and patients' samples between some methods, including routine methods, may be preserved. Thus, these materials can be used to calibrate the routine methods in terms of the corresponding reference methods after commutability has been verified. Current studies suggest that this objective can be reached, provided three criteria are satisfied: i) the calibrated and reference methods must be of equal specificity; ii) the enzyme calibrator should be, as closely as possible, identical to the human analyte enzyme in its native matrix (eg serum); iii) and the inter-method ratio should be constant (within the limits of experimental error) for the enzyme calibrator and for all patients' samples.
...
PMID:Reference materials in clinical enzymology: preparation, requirements and practical interests. 799 75
A total of 10 strains each of Fusobacterium necrophorum subsp. necrophorum and Fusobacterium necrophorum subsp. funduliforme were tested for the production of 13 extracellular enzymes. DNase,
alkaline phosphatase
, and
lipase
were predominantly associated with all the strains of F. necrophorum subsp. necrophorum, with DNase not detected in any of the strains of F. necrophorum subsp. funduliforme. In addition, the strains of F. necrophorum subsp. necrophorum were generally more hemolytic than those of F. necrophorum subsp. funduliforme. Lecithinase, beta-lactamase, elastase, hyaluronidase, chondroitin sulfatase, and coagulase were not detected in any of the strains. DNase may be used to differentiate between the two subspecies.
...
PMID:Comparison of extracellular enzymes of Fusobacterium necrophorum subsp. necrophorum and Fusobacterium necrophorum subsp. funduliforme. 837 Jul 61
Rats were tested in the forced swim test to evaluate the effects of duration of exposure (0, 5, 15, or 25 min), and water temperature (0, 35, 30, 25, or 20 degrees C), on a variety of physiological measures. Serum corticosterone, glucose, lactate, phosphorus levels, and the anion gap (a measure of acid-base status) were increased significantly, whereas carbon dioxide and potassium levels were consistently decreased by testing, as was the potassium/phosphorus ratio; creatinine, triglycerides, and magnesium were not altered significantly in any study. Effects on prolactin, amylase,
lipase
, cholesterol,
alkaline phosphatase
, sodium, and chloride were inconsistent. Levels of serum corticosterone were increased at each duration of testing, and the increments were significantly higher than the previous duration. Corticosterone levels were also increased in proportion to decreasing water temperature, but the increments were not significantly different from the previous or following temperatures. Glucose levels were increased at every duration and at every water temperature with the exception of the coldest water temperature. Lactate and phosphorus levels and the anion gap were all increased, whereas carbon dioxide levels decreased after 5 min of immersion. Potassium levels did not decrease until some time after 5 min of testing. Immobility times were marginally correlated with corticosterone levels (r = -0.38) but were highly correlated with serum carbon dioxide (r = 0.59), potassium (r = 0.67), and phosphorus levels (r = -0.73); the correlation between immobility times and the ratio of potassium/phosphorus was 0.82. The potassium/phosphorus ratio accounted for 67% of the variance in immobility. These high correlations were interpreted in terms of acid-base changes associated with testing.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Physiological correlates of the forced swim test in rats. 837 26
An epidemiologic study of Pasteurella haemolytica serovar 1 (Ph1) in market-stressed feeder calves from 7 farms in eastern Tennessee was conducted. The nasal mucus of each calf was cultured sequentially at the farm of origin (day 0), at an auction market (day 133), and at a feedyard in Texas (days 141, 148, 155, and 169). Of the 103 calves tested, 77 were culture-positive, including 1 on day 0, 1 on day 133, 20 on day 141, 57 on day 148, 50 on day 155, and 14 on day 169. From the 143 Ph1 isolates, 20 enzyme profiles were determined by use of a commercial enzyme system that detects 19 enzymatic reactions; 4 antimicrobial susceptibility profiles were obtained, using the disk-diffusion method, which evaluated susceptibility to 11 antibacterial drugs. All isolates were positive for acid phosphatase and
alkaline phosphatase
, but were negative for alpha-galactosidase, alpha-mannosidase, beta-glucosidase, beta-glucuronidase, cystine aminopeptidase, N-acetyl-beta-glucosaminidase, and trypsin. Other positive enzyme reactions included: leucine aminopeptidase, 140 Ph1 isolates; phosphohydrolase, 90 isolates; alpha-fucosidase, 63 isolates; esterase (C4), 59 isolates; valine aminopeptidase, 30 isolates; esterase
lipase
(C8), 24 isolates; beta-galactosidase, 2 isolates; and alpha-glucosidase, chymotrypsin and
lipase
(C14), 1 isolate each. Thirty-four Ph1 profiles were identified, using combined enzyme and antimicrobial susceptibility profiles. The data indicate that the strains isolated during the feedyard period may have been determined more by farm of origin (P < or = 0.001) than by habitation with calves from other farms while in the feedyard.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Identification of Pasteurella haemolytica A1 isolates from market-stressed feeder calves by use of enzyme and antimicrobial susceptibility profiles. 842 78
Antimicrobial susceptibility of 50 local isolates of Helicobacter pylori from patients with acid peptic diseases was investigated to commonly used antibiotics. The maximum resistance was (66%) detected to metronidazole (MIC > 8 micrograms/ml). The frequency of resistance to ampicillin, erythromycin, ciprofloxacin was in the range of 20-28 per cent; least resistance was observed to tetracycline (10%). The gradient disc diffusion method was found to give reproducible results and also correlated with agar dilution method for minimum inhibitory concentration (MIC). Study of the enzymatic activity of H. pylori isolates showed that all isolates had urease, catalase, oxidase, esterase-
lipase
, and naphthol-AS-beta-1-phosphohydrolase enzymes and were consistently negative for ten other enzymes tested. Majority of the isolates expressed
alkaline phosphatase
(17/18), esterase (17/18) and acid phosphatase (14/18). The acid phosphatase had the maximum mean enzymatic activity. There was no difference in enzymatic activity between H. pylori isolates from ulcer and gastritis patients. H. pylori isolates could be typed into five biotypes. Type III was found to be more common (44.4%). This study supports the existence of the strain variations among H. pylori on the basis of the enzyme profiles.
...
PMID:Antimicrobial susceptibility pattern & biotyping of Helicobacter pylori isolates from patients with peptic ulcer diseases. 855 18
The enzymatic activity of 70 feline and canine Microsporum canis isolates was determined by the Api-Zym test. The liquid phase of cultures, inoculated into Tryptic Soy Broth, was used to examine 19 enzymes. Considerable differences were observed among the extracellular enzymatic patterns. All the isolates produced
alkaline phosphatase
and beta-glucosidase, while
lipase
(C14), trypsin, chymotrypsin, beta-glucuronidase, and alpha-fucosidase activity was never revealed. Esterase (C4) activity was present in 57 samples (81%), esterase
lipase
(C8) in 31 (44%), leucine arylamidase in 35 (50%), valine arylamidase and cystine arylamidase in 7 (10%), acid phosphatase in 64 (91%), naphthol-AS-BI-phosphohydrolase in 60 (86%), alpha-galactosidase in 5 (7%), beta-galactosidase in 6 (8%), alpha-glucosidase in 25 (36%), N-acetyl-beta-glucosaminidase in 41 (58%), and alpha-mannosidase in 51 (73%). The beta-galactosidase activity of M. canis has not been reported previously. Remarkable variations of intensity for each enzymatic activity were also detected. It is believed that these results could provide basic data for further investigations on the pathogenic role of enzymes secreted by M. canis.
...
PMID:Extracellular enzymatic activity of Microsporum canis isolates. 868 26
The stability of 25 analytes from serum of healthy donors was determined at room temperature, 4 degrees C, and -20 degrees C over 48 h, 14 days, and 4 months, respectively. Glucose, blood urea nitrogen, sodium, potassium, chloride, creatinine, calcium, phosphorus, uric acid, total protein, albumin, triglycerides,
lipase
, total creatine kinase, gamma-glutamyltransferase, iron, magnesium, and cholesterol were stable at all three temperatures for the specified times. Carbon dioxide, aspartate and alanine aminotransferases, lactate dehydrogenase, amylase,
alkaline phosphatase
, and high-density lipoprotein cholesterol demonstrated some loss over time. Proper storage temperatures and times must be considered for these analytes if measurement is not to take place immediately after specimen collection.
...
PMID:Stability of twenty-five analytes in human serum at 22 degrees C, 4 degrees C, and -20 degrees C. 870 97
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