New Chromogenic Substrate for Determination of Serum Amylase Activity

1970 ◽  
Vol 16 (1) ◽  
pp. 32-38 ◽  
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.

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.

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.

Determination of Serum Amylase Activity by Amyloclastic Method

2015 ◽  
pp. 65-65
Author(s):  
Arti Pandey ◽  
Arun Pandey ◽  
Naveen Shreevastava ◽  
Durga Neupane
Keyword(s):  
Serum Amylase ◽  
Amylase Activity ◽  
Serum Amylase Activity

scholarly journals Secrets, puzzles and mysteries of macroamylasemia

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.

(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.

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.

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

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

1964 ◽  
Vol 10 (10) ◽  
pp. 891-906 ◽  
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.

Standardization of immunochemical determinations of serum albumin.

1981 ◽  
Vol 27 (5) ◽  
pp. 736-738 ◽  
Author(s):  
J W Keyser ◽  
R Fifield ◽  
G L Watkins
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Normal Human Serum ◽  
Reference Standard ◽  
Protein Nitrogen ◽  
Critical Comparison ◽  
Normal Human ◽  
Theoretical Results

Abstract When we compared four commercially available preparations of human serum albumin with the human serum standard IFCC 74/1 by radial immunodiffusion, by immunoprecipitation turbidimetry, by laser nephelometry, and by "rocket" immunoelectrophoresis, three of the preparations gave almost "theoretical" results with the immunoprecipitation turbidimetric method. Results by the other three methods tended inconsistently to be low. Four pools of normal human serum were also analyzed for albumin by these four immunochemical methods, again with IFCC 74/1 as the reference standard. The results were virtually identical with those obtained by fractionation with 1.8 mol/L sodium sulfate and determination of protein nitrogen in the filtrate. We suggest that a combination of (a) fractionation of a pool of normal human serum in this way and (b) critical comparison with selected commercial preparations of human serum albumin will permit standardization of the serum albumin determination.

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