Determination of amylase activity in serum by using a wheat germ inhibitor with the Du Pont aca.

1986 ◽  
Vol 32 (8) ◽  
pp. 1539-1541 ◽  
Author(s):  
D A Lacher ◽  
M B Harize
Keyword(s):  
Acute Pancreatitis ◽  
Wheat Germ ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Reference Interval ◽  
Pancreatic Amylase ◽  
Wheat Germ Extract ◽  
Rapid Procedure ◽  
Assay Conditions

Abstract A rapid procedure for determining salivary- and pancreatic-type amylase (EC 3.2.1.1) in serum by incorporating a wheat germ inhibitor (from Triticum aestivum) was developed for the Du Pont aca IV analyzer. Under optimal assay conditions, activities of salivary and pancreatic amylase were inhibited by 93% and 19%, respectively. The 95% central reference interval for the percentage of inhibition of serum amylase was 38-84%. Patients with acute pancreatitis showed less than 26% inhibition of amylase after addition of the wheat germ extract, reflecting the prevalence of pancreatic-type amylase in this disorder.

Three methods compared for determination of pancreatic and salivary amylase activity in serum of cystic fibrosis patients.

1986 ◽  
Vol 32 (2) ◽  
pp. 296-300 ◽  
Author(s):  
R O Wolf ◽  
V S Hubbard ◽  
B K Gillard ◽  
A Kingman
Keyword(s):  
Cystic Fibrosis ◽  
Gel Electrophoresis ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Pancreatic Insufficiency ◽  
Polyacrylamide Gel Electrophoresis ◽  
Pancreatic Amylase ◽  
Salivary Amylase ◽  
Amylase Isoenzymes

Abstract We evaluated three methods for serum amylase (EC 3.2.1.1) isoenzymes to determine whether they are interchangeable and to test their ability to discriminate between cystic fibrosis patients with and without pancreatic insufficiency. One method involved salivary amylase inhibitor (O), and two were polyacrylamide gel electrophoresis separations differing in method of detection--either direct zymogram (G) or gel slicing followed by activity estimates per slice (W). Results for percentage pancreatic amylase differed significantly. Reproducibility for percentage pancreatic amylase was high, moderate, and low (r = 0.95, 0.53, and 0.02) for methods G, O, and W, respectively; moderate (r = 0.60) among the three methods; and moderate between pairs. Therefore, this result for a subject must be considered relative to the method used in its determination. The clinical diagnosis of pancreatic insufficiency was verified by 77.8%, 83.3%, and 94.4% correct classification rates for methods O, W, and G, respectively. Evidently, method G is the most efficient and may be the method of choice for measuring serum amylase isoenzymes in cystic fibrosis.

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.

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.

Combined serum amylase and lipase determinations for diagnosis of suspected acute pancreatitis

1993 ◽  
Vol 39 (12) ◽  
pp. 2495-2499 ◽  
Author(s):  
J P Corsetti ◽  
C Cox ◽  
T J Schulz ◽  
D A Arvan
Keyword(s):  
Acute Pancreatitis ◽  
Logistic Regression ◽  
Regression Analysis ◽  
Test Performance ◽  
Serum Amylase ◽  
Discriminant Functions ◽  
Clinical Implementation ◽  
Sensitivity Specificity ◽  
Bivariate Approach

Abstract Serum amylase and lipase measurements are often used to diagnose acute pancreatitis. This study addresses the question of whether it is advantageous to order serum amylase and lipase tests simultaneously. We evaluated performance of the two tests separately and in combination through a retrospective study of patients for whom both amylase and lipase determinations were ordered. Initial analysis of test performance was conducted with a uniformly applied criterion based on determination of optimal sensitivity-specificity pairs. Individual tests and combinations of tests, including the "AND" and "OR" rules and discriminant functions, were examined. Only the discriminant approach demonstrated better performance than the lipase test alone. This finding was subsequently confirmed by logistic regression analysis. We conclude that ordering both tests simultaneously can be advantageous in diagnosing acute pancreatitis when a bivariate approach is used; however, this must be weighed against the difficulties associated with clinical implementation of such approaches.

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.

SOME OBSERVATIONS ON THE PANCREATIC AMYLASE AND INTESTINAL MALTASE OF THE CHICK

1963 ◽  
Vol 41 (1) ◽  
pp. 2107-2121 ◽  
Author(s):  
B. M. Laws ◽  
J. H. Moore
Keyword(s):  
Small Intestine ◽  
Amylase Activity ◽  
Pancreatic Amylase ◽  
Ph Optimum ◽  
Modified Method ◽  
Mucosal Cells ◽  
Small Intestinal ◽  
The Stability ◽  
Hydrolysis Of

The digestive enzymes amylase and maltase were studied in acetone-dried powders or homogenates of the pancreatic and small intestinal tissues and small intestinal contents obtained from chicks of various ages. The stability of pancreatic amylase, which was relatively low in 0.15 M sodium chloride, was increased markedly by the presence of 0.02 M barbiturate buffer. The pH optimum of pancreatic amylase (chloride-activated) was 7.0 whereas that of intestinal maltase was 6.9. High levels of pancreatic amylase activity were found in the newly-hatched chick but these levels decreased during the following 20 days and then remained constant. The contrast between the high amylase and low maltase activities in the contents of the small intestine suggested that molecules of maltose, formed by the hydrolysis of starch, were absorbed as such by the mucosal cells. It appeared that maltose could be absorbed with equal facility from all sections of the small intestine of the 10-day-old chick but in the older birds maltose absorption seemed to occur more readily from the upper small intestine than from the duodenum and lower small intestine. A modified method for the determination of maltase activity is described.

Specific immunoassay of alpha-amylase isoenzymes in human serum.

1985 ◽  
Vol 31 (8) ◽  
pp. 1331-1334 ◽  
Author(s):  
M Gerber ◽  
K Naujoks ◽  
H Lenz ◽  
W Gerhardt ◽  
K Wulff
Keyword(s):  
Monoclonal Antibody ◽  
Human Serum ◽  
Enzyme Immunoassay ◽  
Amylase Activity ◽  
Alpha Amylase ◽  
Pancreatic Amylase ◽  
Routine Method ◽  
Salivary Amylase ◽  
Amylase Isoenzymes

Abstract A monoclonal antibody (66C7) was prepared that specifically binds human salivary amylase (EC 3.2.1.1); it cross reacts with human pancreatic amylase by less than 1%. Two procedures are described for determination of isoamylases in human serum with this antibody: an enzyme immunoassay for determining amylase of salivary origin, and a routine method in which this amylase is immunoprecipitated and the remaining (pancreatic) amylase activity is assayed. Results by the two methods correlate well.

Species difference in pancreatic lipolytic and amylolytic enzymes

1963 ◽  
Vol 18 (1) ◽  
pp. 77-82 ◽  
Author(s):  
Leslie Zieve ◽  
William C. Vogel ◽  
William D. Kelly
Keyword(s):  
Acute Pancreatitis ◽  
Serum Amylase ◽  
Species Difference ◽  
Sharp Contrast ◽  
Pancreatic Amylase ◽  
Amylolytic Enzymes

The pancreatic content of lecithinase A in man is approximately 10–20 times that in the dog. In contrast, the pancreatic content of lipase is one-half and of amylase one-sixth that of the dog. The rabbit is similar to man in its pancreatic amylase and lipase content, and to the dog in its lecithinase A content. In man the serum lecithinase A increases during acute pancreatitis, paralleling more or less the elevations in serum amylase and lipase. Though individual discrepancies are noted, all three enzymes increase roughly proportionately. During acute pancreatitis in the dog, the serum lecithinase A increases but slightly, in sharp contrast to the elevations in serum amylase and lipase which are greater than in man. Submitted on July 12, 1962

scholarly journals Total and Pancreatic Amylase Measured with 2-Chloro-4-nitrophenyl-4-O-β-d-galactopyranosylmaltoside

2000 ◽  
Vol 46 (7) ◽  
pp. 928-933 ◽  
Author(s):  
Yoshitaka Morishita ◽  
Yoshitsugu Iinuma ◽  
Nobuo Nakashima ◽  
Keiichi Majima ◽  
Katsuhiko Mizuguchi ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amylase Activity ◽  
Biological Fluids ◽  
Transfer Reactions ◽  
Pancreatic Amylase ◽  
Salivary Amylase ◽  
Specific Determination ◽  
Routine Procedures

Abstract Background: Many different methods have been used to assay amylase activity, using nitrophenylated oligosaccharides as substrate; however, the hydrolysis steps in these methods are complex. Methods: We developed a new continuously monitoring assay for amylase activity in biological fluids, using 2-chloro-4-nitrophenyl-4-O-β-d-galactopyranosylmaltoside (GalG2CNP) as the substrate; this assay was used with anti-human salivary amylase monoclonal antibodies for specific determination of the pancreatic isoenzyme. Amylase converted GalG2CNP into β-d-galactopyranosylmaltose and 2-chloro-4-nitrophenol, which was measured at 405 nm. Results: GalG2CNP was cleaved between 2-chloro-4-nitrophenol and β-d-galactopyranosylmaltose and did not undergo transfer reactions. The within-assay CVs (n = 20) for total amylase (T-AMY) and pancreatic amylase (P-AMY) were 0.6–1.6% and 0.5–2.5%, respectively; and day-to-day CVs (n = 10) for T-AMY and P-AMY were 0.8–3.7% and 0.6–4.1%, respectively. T-AMY and P-AMY activities in serum or urine obtained by the proposed method correlated well with those determined by the 2-chloro-4-nitrophenyl 4-O-β-d-galactopyranosyl-β-maltotetraoside method or the modified IFCC method. Conclusions: This novel assay for T-AMY and P-AMY measures both activities stoichiometrically, directly, and easily, and may be suitable for routine procedures.

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