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)

Early and appropriate treatment of acute pancreatitis (AP) depends on early causal diagnosis. Published studies have shown favourable results following sphincterotomy performed within the 72 hours of onset of severe gallstone-associated AP. Among the various bio-clinical indices, the lipase/amylase (L/A) ratio, computed within 72 hours after onset, has been shown to discriminate between alcoholic and non alcoholic AP. Our study evaluates the data of biochemical disorders in 51 patients presenting with an episode of AP; these patients were divided into 3 groups: A: alcoholic AP, n = 15; B: biliary AP, n = 25; and C: post-ERCP AP, n = 11. These 3 groups were similar with respect to clinical severity of AP and CT scan. The time delays between onset of the symptoms and the biochemical assay were 1.9 +/- 0.3, 1.9 +/- 0.2 and 0.6 +/- 0.3 d (P < 0.01). AST, ALT, bilirubin, GGT and alkaline phosphatase were significantly (P < 0.05) greater in group B. Blamey's score was 0.5 +/- 0.2, 2.8 +/- 0.2 and 2.5 +/- 0.4 in groups A, B and C respectively. Serum amylase, serum lipase and L/A ratio were identical in groups A and B. The decrease in serum amylase after 48 hours was more important only in group B (56 +/- 8, 80 +/- 4, 47 +/- 3% respectively in groups A, B and C). L/A ratio was significantly greater in group C when compared with group A and B (1.7 +/- 0.4, 1.5 +/- 0.2 and 2.2 +/- 0.3 in groups A, B and C respectively).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Is the identification of acute biliary and alcoholic pancreatitis by early pancreatic enzyme assay possible?]. 751 3

In 403 patients suspected of having pancreatic cancer, we prospectively studied a combination assay of various serum tumor markers: CA19-9, DUPAN2, tissue polypeptide antigen, elastase 1, gamma-glutamyltranspeptidase, lactate dehydrogenase, lipase, amylase, and alkaline phosphatase. The diagnostic value of each marker was compared with a multivariate analysis (computer-aided multivariate and pattern analysis system for pancreatic cancer examine-1: CAMPAS-PX1). Pancreatic cancer was subsequently identified in 47 patients. CAMPAS-PX1 had higher negative in health and positive predictability than those of each marker used alone in the diagnosis of pancreatic cancer. CAMPAS-PX1 proved the most effective marker for diagnosing pancreatic cancer, but in terms of its cost/benefit ration CAMPAS-PX1 was not superior to CA19-9 used alone. In this prospective trial, we experienced poor generalizability in the statistical models (CAMPAS-PX1). We believe that selection bias was present in samples used for model building. Based on this study a new model has been designed.
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PMID:Effectiveness of multivariate analysis of tumor markers in diagnosis of pancreatic carcinoma: a prospective study in multiinstitutions. 753 33

Determination of serum pancreatic enzymes remains the gold standard for the diagnosis of acute pancreatitis. Clinical symptoms and signs are of major importance in suspecting the disease, but they are not accurate enough to confirm the diagnosis. Among pancreatic enzymes, total amylase, pancreatic isoamylase and lipase are preferred, since simple, rapid and unexpensive enzymatic methods are commercially available. More expensive and cumbersome methods (e. g. ELISA for pancreatic elastase) are required if a significant delay to hospital admission occurs. In that case, other serum enzymes are usually normal or only lightly increased. To early define the etiology of acute pancreatic serum pancreatic enzymes lack of value. With this purpose, determination of AST, bilirubin and alkaline phosphatase may allow to distinguish between biliary and non-biliary origin of the disease.
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PMID:Clinical and laboratory diagnosis of acute pancreatitis. 754 60

The growth of group A human, bovine, equine and porcine rotaviruses were enhanced by pretreatment of virus with pancreatin, trypsin, protease, alkaline phosphatase or pepsin and incorporation of these enzymes in maintenance medium. In contrast, alpha-amylase or lipase inhibited the growth of equine and porcine rotaviruses. The other enzymes, adenosine deaminase, lactase, lysozyme, ribonuclease or triose-phosphate isomerase gave little or no change in the growth of all four rotaviruses.
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PMID:Effect of enzymes on the growth of human and animal rotaviruses. 754 24

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.
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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.
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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.
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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.
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PMID:Reference materials in clinical enzymology: preparation, requirements and practical interests. 799 75

A total of 25 apparently healthy adults (13 men and 12 women), 29.5 years (SD = 3.6 years) of age, served as subjects in a 24-h study conducted in Barcelona, Spain, in the spring of 1990. The group had a homogeneous pattern of meals, activity, and behavior. Six blood samples were collected at 4-h intervals over a single 24-h period beginning at 10:00 h. The oral temperature was measured at 2-h intervals to facilitate an independent biological time reference for the local population being studied. The serum concentration of 12 enzymes of clinical interest were measured in each sample: creatine kinase, creatine kinase 2, alanine aminotransferase, aspartate aminotransferase, gamma-glutamyltransferase, alkaline phosphatase, cholinesterase, lactate dehydrogenase, lactate dehydrogenase 1, 5'-nucleotidase, pancreatic alpha-amylase, and triacylglycerol lipase. We supposed that all experimental data obtained for a quantity came from a single "hypothetical subject" that represented the central tendency of the population and then these data were analyzed for circadian rhythm by single cosinor. A statistically significant circadian rhythm was detected in all quantities studied (p < or = 0.05) except for serum concentrations of pancreatic alpha-amylase and triacylglycerol lipase. The maximum daily rhythmic variation was approximately 10% (interval, 6-14%) for all quantities studied except pancreatic alpha-amylase (2.6%). This rhythmic variation is greater than the analytical variation except for 5'-nucleotidase and pancreatic alpha-amylase. The acrophases for the quantities studied (except that of triacylglycerol lipase) coincide with times near those of the oral temperature acrophase (18:01 local time). The results of this study will doubtless contribute to further documentation of the structure of the human circadian timing system and to establishment of time-qualified reference intervals for a defined group of subjects.
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PMID:Circadian rhythms of serum concentrations of 12 enzymes of clinical interest. 810 Apr 88

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.
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PMID:Comparison of extracellular enzymes of Fusobacterium necrophorum subsp. necrophorum and Fusobacterium necrophorum subsp. funduliforme. 837 Jul 61


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