A New Saccharogenic Micromethod for Measurement of Amylase Activity in Biological Fluids

1970 ◽  
Vol 16 (4) ◽  
pp. 300-304 ◽  
Author(s):  
Klaus Lorentz ◽  
Detlef Oltmanns
Keyword(s):  
Standard Deviation ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Biological Fluids ◽  
Soluble Starch ◽  
Starch Digestion ◽  
Triphenyltetrazolium Chloride ◽  
Serum Amylase Activity ◽  
Apparently Healthy

Abstract To determine serum amylase activity we have quantitatively measured the glucose and maltose hydrolyzed from soluble starch by colorimetrically measuring the reduction of colorless triphenyltetrazolium chloride to a red formazan, which is dissolved in methanol. The method is suitable for use with microsamples of all biological fluids, and is specific for the final products of starch digestion. Values found for sera from 55 apparently healthy blood donors ranged from 0.15 to 1.55 (mean, 0.83; standard deviation, ±0.4) mg of glucose per ml per h, corresponding to 7.5 to 78 Somogyi units.

An Automated, Saccharogenic Method for Determining Serum Amylase Activity

1970 ◽  
Vol 16 (12) ◽  
pp. 985-989 ◽  
Author(s):  
Wendell R O'Neal ◽  
Nathan Gochman
Keyword(s):  
Glucose Oxidase ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Serum Glucose ◽  
Normal Range ◽  
Reducing Substances ◽  
Serum Amylase Activity

Abstract An automated adaptation of the Somogyi saccharogenic determination of serum amylase is described in which conventional AutoAnalyzer modules are used. Adequate sensitivity with short incubation is achieved by incorporating glucose oxidase and catalase in the substrate to destroy serum glucose during incubation. Maltose and other dialyzable oligosaccharides are measured with the alkaline copper-neocuproine reaction. A simultaneous blank run is performed to determine reducing substances other than glucose in serum. Precision studies and correlation with a manual saccharogenic method are presented. The normal range was determined from data for 49 healthy blood donors.

(Washington University case conference): acute pancreatitis, hyperlipemia, and normal amylase.

1978 ◽  
Vol 24 (5) ◽  
pp. 815-820 ◽  
Keyword(s):  
Acute Pancreatitis ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Normal Serum ◽  
Case Conference ◽  
Diagnosis And Management ◽  
Serum Amylase Activity ◽  
Washington University

Abstract This case focuses on the biochemical findings in acute pancreatitis and the role of the laboratory in the diagnosis and management of such patients. It also illustrates a major unappreciated problem in the use of amylase determinations in patients with acute pancreatitis: normal serum amylase activity in the presence of hyperlipemia.

Effect of Cadmium Exposure on Serum Amylase Activity in Cadmium Electroplating Workers

2006 ◽  
Vol 1 (4) ◽  
pp. 260-267 ◽  
Author(s):  
R. B. Kalahasthi ◽  
Rajmohan Hirehal Raghavendra Rao ◽  
Rajan Bagalur Krishna Murthy ◽  
M. Karuna Kumar
Keyword(s):  
Serum Amylase ◽  
Amylase Activity ◽  
Cadmium Exposure ◽  
Serum Amylase Activity

scholarly journals Modified Form of the Fibrinogen Bβ Chain (des-Gln Bβ), a Potential Long-Lived Marker of Pancreatitis

2007 ◽  
Vol 53 (12) ◽  
pp. 2105-2111 ◽  
Author(s):  
David Schmidt ◽  
Stephen O Brennan
Keyword(s):  
Plasma Sample ◽  
Serum Amylase ◽  
Peptide Mapping ◽  
Amylase Activity ◽  
Pancreatic Disease ◽  
Reversed Phase ◽  
Ionization Mass ◽  
Carboxypeptidase A ◽  
Serum Amylase Activity

Abstract Background: During an investigation of genetic variants of fibrinogen, we observed a novel form of the Bβ chain, with a mass decrease of approximately 128 Da, in one of the controls. The plasma sample originated from an individual who had experienced acute pancreatitis a week earlier but whose serum amylase activity had returned to normal. We investigated the structure of the modified fibrinogen and explored its relationship to pancreatic disease. Method: Fibrinogen was isolated from the plasma of 9 individuals with increased pancreatic amylase activity (114–1826 U/L) and presumed pancreatitis and from 6 control individuals with amylase activities <56 U/L. Fibrinogen (or fibrin) Bβ chains were isolated by reversed-phase HPLC and analyzed directly by electrospray ionization mass spectrometry. Tryptic and CNBr peptide mapping and thrombin treatment pinpointed the location of the 128-Da loss in mass. Results: The acquired fibrinogen Bβ chain modification was attributable to the loss of its C-terminal glutamine residue. Incubating purified fibrinogen with pancreatic carboxypeptidase A (CpA) produced an identical modification. The des-Gln Bβ fibrinogen accounted for >80% of the Bβ chains in 3 of the individuals with increased amylase but only approximately 5% of the Bβ chains in control samples. Conclusion: Pancreatic CpA activity is used as an index of acute pancreatic disease, but given that the circulatory half-lives of fibrinogen and CpA are approximately 4 days and only 2.5 h, respectively, measuring des-Gln Bβ fibrinogen, the in vivo product of CpA activity, could provide clinicians with retrospective evidence of disease.

Effect of nickel exposure on serum amylase activity in nickel-plating workers

2008 ◽  
Vol 90 (2) ◽  
pp. 393-400
Author(s):  
Ravi Babu Kalahasthi ◽  
Rajmohan Hirehal Raghavendra Rao ◽  
Rajan Bagalur Krishna Murthy ◽  
M. Karuna Kumar
Keyword(s):  
Serum Amylase ◽  
Amylase Activity ◽  
Nickel Plating ◽  
Nickel Exposure ◽  
Serum Amylase Activity

Reinterpretation of Hyperamylasemia in Diabetic Coma

1974 ◽  
Vol 20 (6) ◽  
pp. 673-675 ◽  
Author(s):  
David M Goldberg ◽  
Richard J Spooner ◽  
Anthony H Knight
Keyword(s):  
Acid Phosphatase ◽  
Normal Limit ◽  
Serum Amylase ◽  
Acute Viral Hepatitis ◽  
Amylase Activity ◽  
Diabetic Coma ◽  
Glucuronidase Activity ◽  
Normal Human Liver ◽  
Normal Human ◽  
Serum Amylase Activity

Abstract Serum enzyme activity was sequentially determined in 10 consecutive patients with diabetic ketoacidosis, of whom all had increased β-glucuronidase activity, eight had increased amylase activity, and four had increased acid phosphatase activity. Activity of amylase and that of the two lysosomal enzymes were poorly correlated, irrespective of whether peak activities or activities of all samples were considered. Of 37 cases with acute viral hepatitis, serum β-glucuronidase activity was increased in 33 and amylase activity in four, and the correlation between the two was poor. Study of normal human liver showed that the ratio of its mean enzymatic activity to the upper normal limit for serum was less than 1.0 for amylase, and approximately 80 and 6000 for acid phosphatase and β-glucuronidase, respectively. The hepatocyte cannot be the source of an increased serum amylase activity, and we question whether lysosomes are concerned in its release from other tissues.

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