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Journal of Innovation in Health... Oct 2017Amylase and lipase, pancreatic biomarkers, are measured in acute pancreatitis diagnosis. Since amylase testing does not add diagnostic value, lipase testing alone is...
BACKGROUND
Amylase and lipase, pancreatic biomarkers, are measured in acute pancreatitis diagnosis. Since amylase testing does not add diagnostic value, lipase testing alone is recommended. Despite new recommendations, many physicians and staff continue to test both amylase and lipase.
OBJECTIVE
To reduce unnecessary diagnostic testing in acute pancreatitis.
METHODS
The pre-checked amylase test within the Emergency Department's Computerized Provider Order Entry (CPOE) abdominal pain order set was changed to an un-checked state, but kept as an option to order with a single click. Amylase testing, lipase testing and cost were measured for one year pre and post intervention.
RESULTS
Simple de-selection intervention reduced redundant amylase testing from 71% to 9%, resulting in a percent of decrease of 87% and an annualized saving of approximately $719,000 in charges.
CONCLUSION
CPOE de-selection is an effective tool to reduce non-value added activity and reduce cost while maintaining quality patient care and physician choice.
Topics: Acute Disease; Amylases; Cost Savings; Diagnostic Tests, Routine; Emergency Service, Hospital; Humans; Medical Order Entry Systems; Pancreatitis; Physicians; Quality Improvement
PubMed: 29121848
DOI: 10.14236/jhi.v24i3.907 -
Journal of Immunoassay 1983A sensitive sandwich enzyme immunoassay has been developed for quantitation of alpha-amylase in pig pancreas. The alpha-amylase-antibody conjugate was prepared from... (Comparative Study)
Comparative Study
A sensitive sandwich enzyme immunoassay has been developed for quantitation of alpha-amylase in pig pancreas. The alpha-amylase-antibody conjugate was prepared from horseradish peroxidase coupled with antibodies to hog pancreas alpha-amylase. With this method the measuring range is 1-10 ng/ml and the detection limit is 0.2 ng/ml. The amount of pig pancreatic amylase was measured to be 6.21 +/- 2.05 mg/g of tissue. The enzymatic activity determination and immunoassay were compared in the material studied.
Topics: Amylases; Animals; Enzyme-Linked Immunosorbent Assay; Immunoenzyme Techniques; Pancreas; Rabbits; Swine; alpha-Amylases
PubMed: 6193146
DOI: 10.1080/15321818308057005 -
Annals of Surgery Mar 1975Thirty-four patients with abdominal pain, tenderness, and hyperamylasemia suggesting acute pancreatitis were studied prospectively to elucidate the relationship between... (Comparative Study)
Comparative Study
Thirty-four patients with abdominal pain, tenderness, and hyperamylasemia suggesting acute pancreatitis were studied prospectively to elucidate the relationship between peptic ulcer disease and pancreatitis. Confirming evidence of pancreatitis and/or ulcer was obtained either at laparotomy of by upper gastrointestinal roentgenograms. The presence or absence of pancreatitis was substantiated by measurement of the amylase/creatinine clearance ratio, which is significantly higher (p less than 0.001) in patients with acute pancreatitis (9.3 plus or minus 0.9), than in patients without pancreatitis (3.1 plus or minus 0.2). Nine of the 34 patients were found to have gastric or duodenal ulcers. However, seven of the nine, despite an elevated serum amylase, had no sign of pancreatitis at surgery, on radiological examination, or by elevation of the amylase/creatinine clearance ratio (3.1 plus or minus 0.4). It is suggested that hyperamylasemia associated with peptic ulcer disease is most often not indicative of acute pancreatitis and that treatment is most appropriately directed at the ulcer.
Topics: Acute Disease; Amylases; Creatinine; Diagnosis, Differential; Duodenal Ulcer; Humans; Pancreatitis; Peptic Ulcer; Stomach Ulcer
PubMed: 1130848
DOI: 10.1097/00000658-197503000-00012 -
Journal of Dental Research 1969
Topics: Amylases; Spectrophotometry
PubMed: 5254492
DOI: 10.1177/00220345690480032701 -
Journal of Bacteriology Dec 1945
Topics: Amylases; Bacteria; Humans
PubMed: 21011728
DOI: 10.1128/JB.50.6.711-714.1945 -
BMC Microbiology Mar 2014Environmental screening programs are used to find new enzymes that may be utilized in large-scale industrial processes. Among microbial sources of new enzymes, the...
BACKGROUND
Environmental screening programs are used to find new enzymes that may be utilized in large-scale industrial processes. Among microbial sources of new enzymes, the rationale for screening fungal endophytes as a potential source of such enzymes relates to the hypothesised mutualistic relationship between the endophyte and its host plant. There is a need for new microbial amylases that are active at low temperature and alkaline conditions as these would find industrial applications as detergents.
RESULTS
An α-amylase produced by Preussia minima, isolated from the Australian native plant, Eremophilia longifolia, was purified to homogeneity through fractional acetone precipitation and Sephadex G-200 gel filtration, followed by DEAE-Sepharose ion exchange chromatography. The purified α-amylase showed a molecular mass of 70 kDa which was confirmed by zymography. Temperature and pH optima were 25°C and pH 9, respectively. The enzyme was activated and stabilized mainly by the metal ions manganese and calcium. Enzyme activity was also studied using different carbon and nitrogen sources. It was observed that enzyme activity was highest (138 U/mg) with starch as the carbon source and L-asparagine as the nitrogen source. Bioreactor studies showed that enzyme activity was comparable to that obtained in shaker cultures, which encourages scale-up fermentation for enzyme production. Following in-gel digestion of the purified protein by trypsin, a 9-mer peptide was sequenced and analysed by LC-ESI-MS/MS. The partial amino acid sequence of the purified enzyme presented similarity to α-amylase from Magnaporthe oryzae.
CONCLUSIONS
The findings of the present study indicate that the purified α-amylase exhibits a number of promising properties that make it a strong candidate for application in the detergent industry. To our knowledge, this is the first amylase isolated from a Preussia minima strain of endophytic origin.
Topics: Amylases; Ascomycota; Calcium; Chemical Fractionation; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Liquid; Endophytes; Enzyme Activators; Enzyme Stability; Fermentation; Fungal Proteins; Hydrogen-Ion Concentration; Manganese; Mass Spectrometry; Molecular Weight; Sequence Analysis, Protein; Sequence Homology, Amino Acid; Substrate Specificity; Temperature
PubMed: 24602289
DOI: 10.1186/1471-2180-14-55 -
Nihon Rinsho. Japanese Journal of... 1973
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Molecular Biology Reports Feb 2019A synthetic cDNA-AmyA gene was cloned and successfully expressed in Pichia pastoris as a His-tagged enzyme under the methanol inducible AOX1 promoter. High level of...
A synthetic cDNA-AmyA gene was cloned and successfully expressed in Pichia pastoris as a His-tagged enzyme under the methanol inducible AOX1 promoter. High level of extracellular amylase production of 72 U/mL was obtained after a 72 h induction by methanol. As expected, the recombinant strain produced only the AmyA isoform since the host is a protease deficient strain. Besides, the purified r-AmyA showed a molecular mass of 54 kDa, the same pH optimum equal to 5.6 but a higher thermoactivity of 60 °C against 50 °C for the native enzyme. Unlike AmyA which maintained 50% of its activity after a 10-min incubation at 60 °C, r-AmyA reached 45 min. The higher thermoactivity and thermostability could be related to the N-glycosylation. The r-AmyA activity was enhanced by 46% and 45% respectively in the presence of 4 mM Fe and Mg ions. This enzyme was more efficient in bread-making since such ions were reported to have a positive impact on the nutriment quality and the rheological characteristics of the wheat flour dough. The thermoactivity/thermostability as well as the iron and magnesium activations could also be ascribed to the presence of an additional C-terminal loop containing the His tag.
Topics: Amylases; Aspergillus oryzae; Binding Sites; Computer Simulation; Enzyme Stability; Gene Expression Regulation, Enzymologic; Histidine; Hydrogen-Ion Concentration; Metals; Models, Molecular; Oligopeptides; Pichia; Recombinant Proteins; Temperature
PubMed: 30535895
DOI: 10.1007/s11033-018-4548-2 -
Gut Jan 1977The amylase creatinine clearance ratio (ACCR) is considered to be a more sensitive index of acute pancreatitis than the serum amylase level. Serial ACCR estimations were... (Comparative Study)
Comparative Study
The amylase creatinine clearance ratio (ACCR) is considered to be a more sensitive index of acute pancreatitis than the serum amylase level. Serial ACCR estimations were undertaken in 25 patients undergoing an elective cholecystectomy. Using accepted criteria, 28% of these patients developed, in the postoperative period, biochemical evidence of pancreatic gland damage, although the serum amylase level remained normal. This raised ACCR was particularly noted in patients who had undergone an exploration of the common bile duct. The ACCR would appear to be a more sensitive index of pancreatic gland disruption secondary to biliary surgery than the serum amylase level.
Topics: Acute Disease; Amylases; Biliary Tract Surgical Procedures; Clinical Enzyme Tests; Creatinine; Humans; Pancreatitis; Postoperative Complications; Prospective Studies; Scotland
PubMed: 402305
DOI: 10.1136/gut.18.1.16 -
Annals of Clinical Biochemistry Nov 1974A plate-diffusion technique for the quantitative assay of amylase in body fluids is described which is dependent on the incorporation of a soluble amylopectin-dye... (Comparative Study)
Comparative Study
A plate-diffusion technique for the quantitative assay of amylase in body fluids is described which is dependent on the incorporation of a soluble amylopectin-dye complex into agar. The technique correlates well with other established amylase assays, and has a coefficient of variation of 1.45 for amylase levels within the normal range for serum. Normal levels of amylase in serum and urine are reported which agree with those recorded by previous workers, and in addition values of amylase in semen, saliva, and tears are quoted.
Topics: Amylases; Analysis of Variance; Evaluation Studies as Topic; Humans; Indicators and Reagents; Methods; Saliva; Semen; Tears
PubMed: 4460844
DOI: 10.1177/000456327401100165