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Pancreatology : Official Journal of the... 2017The measurement of duodenal amylase by a colorimetric end-point assay has been the most used method for amylase activity analyses. The method is manual, time consuming...
OBJECTIVE
The measurement of duodenal amylase by a colorimetric end-point assay has been the most used method for amylase activity analyses. The method is manual, time consuming and dependent on specialized equipment. In this study, we compare an automated kinetic spectrophotometric method for pancreatic amylase measurement in duodenal juice with a standardized colorimetric end-point assay.
METHODS
We used specimen of duodenal juice at random from a biobank obtained by short endoscopic secretin test in patients with suspected exocrine pancreatic failure of different reasons. Duodenal juice was tested for amylase activity with a conservative manual colorimetric endpoint assay (Phadebas Amylase test, Magle AB) and an automated enzymatic kinetic spectrophotometric method using standard reagents for pancreatic amylase activity for Cobas c111 (Roche Diagnostics).
RESULTS
52 samples for assay of amylase were analyzed in pairs. Correlation between measurements with the two methods was r = 0.99 (p < 0.001), linear regression 0.99 (p < 0.001).
CONCLUSION
Quantification of duodenal amylase activity with automated spectrophotometry has excellent correlation to measurements made by the manual method. This allows for standardized, center independent analyses of duodenal amylase for the assessment of acinar pancreatic function.
Topics: Amylases; Automation; Colorimetry; Humans; Pancreatic Juice; Sensitivity and Specificity; Spectrophotometry
PubMed: 28190684
DOI: 10.1016/j.pan.2017.02.001 -
Clinica Chimica Acta; International... Mar 1976Isozymes of human pancreatic alpha-amylase were used as immunogens to raise antisera in rabbits. These antisera were unable to differentiate between the two isoamylases...
Isozymes of human pancreatic alpha-amylase were used as immunogens to raise antisera in rabbits. These antisera were unable to differentiate between the two isoamylases but produced an almost total inhibition of serum amylase activity when used at a dilution of 1 : 5000. Similar inhibition patterns were produced with the salivary and urinary enzymes as well as with serum from a patient with acute pancreatitis. No cross reactivity of the antisera with hog pancreatic amylase was observed and only at antiserum concentrations of 1 : 5000 and above was ther any inhibition of monkey serum amylase. The degree of inhibition observed varied with the size of the substrate but was not increased by the use of a second antibody.
Topics: Amylases; Animals; Antibody Formation; Binding Sites, Antibody; Cross Reactions; Haplorhini; Humans; Isoenzymes; Pancreas; Pancreatitis; Rabbits; Saliva; Species Specificity; Structure-Activity Relationship; Swine
PubMed: 813916
DOI: 10.1016/0009-8981(76)90254-0 -
Annals of Surgery Oct 1948
Topics: Amylases; Humans
PubMed: 17859223
DOI: 10.1097/00000658-194810000-00003 -
Biotechnology and Applied Biochemistry Apr 2023Amylases are one of the main enzymes used in various industries such as food, fermentation, textile, and pharmaceuticals. Microorganisms are the potent sources of...
Amylases are one of the main enzymes used in various industries such as food, fermentation, textile, and pharmaceuticals. Microorganisms are the potent sources of amylase enzyme, apart from plant and animal sources. Fungal amylases are more stable than bacterial amylases. The production of extracellular α-amylase from Aspergillus tamarii MTCC5152 using solid-state and submerged fermentation (SSF and SmF) and the various nutritional factors influencing its production were studied. A higher activity of α-amylase (519.40 u/g) was attained in a medium having wheat bran (WB) alone as the substrate at an initial moisture content of 70% (v/w) with 2.5% (v/w) of inoculum level (containing 10 spores/ml) after 4 days of incubation at 28°C by SSF. Addition of 1% glucose to WB containing basal medium enhanced α-amylase production (6.49 u/ml) after 4 days of incubation by SmF method. Comparative evaluation of enzyme production by SSF and SmF methods produced better results in SSF method.
Topics: alpha-Amylases; Fermentation; Aspergillus; Amylases
PubMed: 36070879
DOI: 10.1002/bab.2403 -
Sheng Wu Gong Cheng Xue Bao = Chinese... Apr 2012Alkaline amylase is one of alkaline enzymes with optimum pH in the alkaline range, and it could keep stability and efficiently hydrolyze starch under alkaline... (Review)
Review
Alkaline amylase is one of alkaline enzymes with optimum pH in the alkaline range, and it could keep stability and efficiently hydrolyze starch under alkaline conditions. Alkaline amylase finds wide applications in textile, detergent, pharmaceutical, food and other fields. Alkaline amylases could be produced by alkaliphilic microorganisms. In this work, the advances of alkaline amylase production and applications were reviewed.
Topics: Amylases; Enzyme Stability; Hydrogen-Ion Concentration
PubMed: 22803393
DOI: No ID Found -
Journal of Biochemistry Feb 1963
Topics: Amylases; Cellulose; Chromatography; alpha-Amylases
PubMed: 13985239
DOI: 10.1093/oxfordjournals.jbchem.a127664 -
Archives of Surgery (Chicago, Ill. :... Aug 1972
Topics: Abdominal Injuries; Adult; Amylases; Debridement; Drainage; Duodenum; Humans; Pancreas; Pancreatectomy; Pancreatitis; Postoperative Complications
PubMed: 5044541
DOI: 10.1001/archsurg.1972.04180080014003 -
The Journal of Biological Chemistry Nov 1950
Topics: Amylases; beta-Amylase
PubMed: 14794706
DOI: No ID Found -
Nature Apr 1961
Topics: Amylases; beta-Amylase
PubMed: 13701729
DOI: 10.1038/190445a0 -
Indian Journal of Experimental Biology Apr 1979
Topics: Amylases; Humans; Male; Oligospermia; Semen; Vasectomy
PubMed: 489072
DOI: No ID Found