Determination of Serum Amylase Activity by Amyloclastic Method

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.

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New Chromogenic Substrate for Determination of Serum Amylase Activity

Clinical Chemistry ◽

10.1093/clinchem/16.1.32 ◽

1970 ◽

Vol 16 (1) ◽

pp. 32-38 ◽

Cited By ~ 41

Author(s):

Bernard Klein ◽

James A Foreman ◽

Ronald L Searcy

Keyword(s):

Enzyme Activity ◽

Human Serum ◽

Serum Amylase ◽

Amylase Activity ◽

Chromogenic Substrate ◽

Excellent Correlation ◽

Rapid Assay ◽

Normal Human ◽

Serum Amylase Activity

Abstract A rapid assay for serum amylase activity has been developed based on the use of a new chromogenic substrate—Cibachron Blue—amylose. The procedure requires 0.1 ml of serum and measures the production of soluble chromogen, the formation of which is linear with enzyme activity. Normal human serum has a mean amylase activity of 118 ± 37 (SD) mg dye/100 ml/15 min or, in international units, 78 ± 24 (SD) µg dye/min/ml. Excellent correlation was observed with a saccharometric amylase procedure.

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Secrets, puzzles and mysteries of macroamylasemia

Herald of Pancreatic Club ◽

10.33149/vkp.2020.01.02 ◽

2020 ◽

Vol 46 (1) ◽

pp. 12-22

Author(s):

N. B. Gubergrits ◽

N. V. Byelyayeva ◽

G. M. Lukashevich ◽

T. L. Mozhyna

Keyword(s):

Serum Amylase ◽

Amylase Activity ◽

Clinical Manifestations ◽

Specific Treatment ◽

Normal Serum ◽

Amylase Level ◽

Clearance Ratio ◽

Urine Amylase ◽

Classical Constant

Physiological features of amylase synthesis and excretion are considered in the article, presence of other sources of amylase synthesis different from pancreas and salivary glands is emphasized. Definitions of hyperenzymemia and macroamylasemia (MAE) are given. MAE is a state characterized by presence of circulating complexes of normal serum amylase with protein or carbohydrates in blood. There are 3 types of MAE: first — classical (constant hyperamylasemia, decreased amylase level in urine, high blood concentration of macroamylase complexes); second — hyperamylasemia with slightly decreased amylase activity in urine, macroamylase/normal amylase ratio is less than in the first type; third — normal blood and urine amylase activity, low macroamylase/normal amylase ratio. Pathogenesis is explained by connection of blood amylase and acute phase protein in different inflammatory, infectious diseases, malabsorption. MAE clinical manifestations could be absent, sometimes abdominal pain is possible. Hyperamylasemia and reduced urine amylase activity are typical. MAE diagnostics means determination of macroamylase complexes in blood (chromatography, calculation of the clearance ratio of amylase and creatinine). The article presents clinical cases describing extra-pancreatic MAE in women with malignant ovarian lesions. The question of expediency of thorough diagnostic examination in asymptomatic MAE is raised, which may turn out to be a symptom of cancer. The lack of specific treatment for MAE is emphasized.

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

Clinical Chemistry ◽

10.1093/clinchem/24.5.815 ◽

1978 ◽

Vol 24 (5) ◽

pp. 815-820 ◽

Cited By ~ 2

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.

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

Clinical Chemistry ◽

10.1093/clinchem/16.4.300 ◽

1970 ◽

Vol 16 (4) ◽

pp. 300-304 ◽

Cited By ~ 5

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.

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

Environmental Bioindicators ◽

10.1080/15555270601025758 ◽

2006 ◽

Vol 1 (4) ◽

pp. 260-267 ◽

Cited By ~ 2

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

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A Study of the Starch-Iodine Complex: A Modified Colorimetric Micro Determination of Amylase in Biologic Fluids

Clinical Chemistry ◽

10.1093/clinchem/10.10.891 ◽

1964 ◽

Vol 10 (10) ◽

pp. 891-906 ◽

Cited By ~ 30

Author(s):

N R Pimstone

Keyword(s):

Serum Amylase ◽

Serum Proteins ◽

Amylase Activity ◽

Optimal Conditions ◽

Serum Factor ◽

Serum Factors ◽

Iodine Complex ◽

Human Sera ◽

Initial Depression

Abstract The limitations, inaccuracies, and practical difficulties of saccharogenic methods are discussed. A modified colorimetric microdetermination of amylase is described in which the digestion of starch is measured by the decrease in the starch-iodine color. Experimental data show that there are two other serum factors that can also cause a fall-off in color: (1) an immediate 10-15% depression of color, probably due to serum proteins and countered by using serum in the control; (2) an acid-serum factor causing a progressive fall-off in color subsequent to the initial depression. Iodine prevents this, and must be added as soon as the acid has been added to stop the enzyme activity. Results of 189 consecutive assays of human sera are presented. Amylase activity of duodenal aspirate has been determined simultaneously by the method described and the Lagerlöf method. Results are compared. Changes in serum amylase and lipase levels in artificially produced pancreatitis in dogs are presented. Optimal conditions for amylase activity are reviewed, and in the light of these, different amyloclastic methods and their results compared. Achroic-point technics are briefly evaluated.

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Microdetermination of Serum Amylase Activity utilizing the 3, 6-Dinitrophthalic Acid Method of Determining Reducing Sugar

YAKUGAKU ZASSHI ◽

10.1248/yakushi1947.94.1_138 ◽

1974 ◽

Vol 94 (1) ◽

pp. 138-143 ◽

Cited By ~ 3

Author(s):

MASATAKE IWASAKI ◽

MUTSUKO OTA ◽

YOSHITAKA OTANI

Keyword(s):

Serum Amylase ◽

Amylase Activity ◽

Reducing Sugar ◽

Acid Method ◽

Serum Amylase Activity

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

Clinical Chemistry ◽

10.1373/clinchem.2007.093179 ◽

2007 ◽

Vol 53 (12) ◽

pp. 2105-2111 ◽

Cited By ~ 9

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.

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