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.

Quantitative gel-electrophoretic determination of serum amylase isoenzyme distributions.

1979 ◽  
Vol 25 (11) ◽  
pp. 1919-1923 ◽  
Author(s):  
B K Gillard
Keyword(s):  
Differential Diagnosis ◽  
Disease Progression ◽  
Quantitative Method ◽  
Serum Amylase ◽  
Soluble Starch ◽  
Normal Serum ◽  
Polyacrylamide Gel ◽  
Starch Solution ◽  
Amylase Isoenzymes

Abstract I report a direct, sensitive, quantitative method for determining serum amylase isoenzyme activity with commercially available reagents. Day-to-day reproducibility (CV) was 3--4% for the isoenzymes in normal serum; within-run precision was 8, 3, and 2% for low, normal and high isoenzyme activities. Amylase isoenzymes, separated into the pancreatic and salivary types by electrophoresis in polyacrylamide gel, are then quantified by directly incubating the gels in soluble-starch solution, staining with iodine, and densitometry. The proportion of pancreatic isoenzyme (47 normal sera) was 43 +/- 8% (mean +/- SD). Isoenzyme activities as low as 2% of normal can be measured accurately in 10 micro L of serum. The reproducibility, precision, and sensitivity indicate that the method is applicable to differential diagnosis of hyperamylasemia or hypoamylasemia, and is suited for monitoring the subtle changes in serum amylase isoenzyme distribution that may accompany disease progression or therapy.

(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.

Determination of Serum and Urine Amylase with Use of Procion Brilliant Red M-2BS Amylopectin

1971 ◽  
Vol 17 (4) ◽  
pp. 311-315 ◽  
Author(s):  
Sylvan M Sax ◽  
Anna B Bridgwater ◽  
John J Moore
Keyword(s):  
Amylase Activity ◽  
Reference Method ◽  
Monomethyl Ether ◽  
Final Solution ◽  
Salivary Amylase ◽  
Ethylene Glycol Monomethyl Ether ◽  
Glycol Monomethyl Ether ◽  
Urine Amylase ◽  
Pancreatic Extract

Abstract We describe a sensitive, precise assay of serum or urine amylase activity, with use of a new substrate, Procion Brilliant Red M-2BS—Amylopectin. After 0.2 ml of serum or urine is incubated with substrate for 10 min at 37°C, ethylene glycol monomethyl ether is added to precipitate proteins and larger substrate particles. Clarity and chromogenicity of the final solution are not sensitive to small changes in temperature or concentrations of the various reagents. No interferences necessitating preparation of specimen blanks have been encountered. Human salivary amylase, assayed by a reference saccharogenic method, is used for calibration. When read against the resulting curve, normal sera and urines give activities comparable to those obtained with the reference method. Human pancreatic extract, sera and urines from pancreatitis patients, and macroamylasemia serum show higher activities by the proposed method.

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.

scholarly journals PANCREATIC CANCER IN 31 YEARS OLD PATIENT WITH NORMAL SERUM AMYLASE LEVEL (Kanker Pankreas di Pasien Usia 31 Tahun dengan Kadar Amilase Serum Normal)

2018 ◽  
Vol 23 (1) ◽  
pp. 96
Author(s):  
Melda F. Flora ◽  
Budiono Raharjo ◽  
Maimun Z. Arthamin
Keyword(s):  
Serum Amylase ◽  
Normal Serum ◽  
Amylase Level ◽  
Gamma Glutamyl Transferase ◽  
Range Limit ◽  
Resonance Imaging ◽  
Serum Amylase Level ◽  
Magnetic Resonance Imaging Mri ◽  
Glutamyl Transferase ◽  
Tomography Scan

Kanker pankreas adalah keganasan sel di jaringan pankreas. kejadiannya meningkat pada usia di atas 60 tahun. Namun, sekitar20% dapat terjadi di usia muda. Patogenesis terjadinya masih belum jelas, dikemukakan bahwa mutasi genetik dan faktor eksogen sepertimerokok berhubungan dengan terjadinya keganasan sel pankreas. Kasus adalah seorang laki-laki perokok berusia 31 tahun dengankeluhan utama nyeri ulu hati menjalar ke punggung, disertai mual, muntah, nafsu makan turun. Pada pemeriksaan fisik didapatkansklera ikterik, perkusi redup dan ronkhi di paru, distensi abdomen dan asites. Pada pemeriksaan laboratorik didapatkan leukositosis,trombositopenia, peningkatan aspartate aminotransaminase (AST) lebih dari 10 kali Upper Range Limit (URL), hiperbilirubinemiadirek, peningkatan alkaline phosphatase (ALP), Gamma Glutamyl Transferase (GGT) dan lipase serum, sedangkan amilase serumnormal. Terdapat juga peningkatan kadar CA19-9. Pada computed tomography scan (CT scan) dan Magnetic Resonance Imaging (MRI)didapatkan gambaran kanker pankreas primer yang telah bermetastasis ke pleura dan hati. Kadar amilase normal di pasien dapatdisebabkan karena awal peningkatan dan penurunan kadar amilase terjadi lebih cepat dan pada saat diperiksa telah turun mencapaikadar normal. Simpulan, kanker pankreas dapat terjadi di usia muda. Amilase yang normal dapat terjadi di kanker pankreas.

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.

Sex-related Differences in Effect of Ethanol Administration and Folic Acid Supplementation on Pancreatic Amylase in Rats

2004 ◽  
Vol 74 (1) ◽  
pp. 64-73
Author(s):  
García-Benítez ◽  
Delgado-Villa ◽  
Murillo ◽  
Carreras
Keyword(s):  
Folic Acid ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Ethanol Consumption ◽  
Folic Acid Supplementation ◽  
Ethanol Administration ◽  
Pancreatic Amylase ◽  
Acid Supplementation ◽  
Urine Amylase ◽  
Advantageous Effect

The present study was designed to determine whether folic acid supplement is sufficient to reverse the negative effects of ethanol consumption on amylase activity during gestation, lactation, and growth. Moreover, this study investigated the sex-related differences in amylase content in the pancreatic tissue, serum, and urine. The animals were randomized into three groups: Control group (CG) received water and a basic rat diet during pregnancy, lactation, and growth; Ethanol-rats (EG) were fed an ethanol diet during pregnancy, the suckling period, and growth until death; and Ethanol + folic acid group (E + FG) were handled the same way as those of EG, except they received a folic acid supplement from reproduction until the end of experimental period. Our results showed that ethanol consumption decreased the pancreatic amylase level in offspring rats at 2 months postpartum. Folic acid supplementation did not alter pancreatic amylase activities. In offspring males, ethanol administration decreased serum amylase activity at 2 months postpartum. Folic acid supplementation in males resulted in higher serum amylase levels than those corresponding to the ethanol-fed group. In females, no significant differences between groups in serum amylase levels were found. Ethanol consumption decreased urinary amylase excretion (at 30 days and 2 months postpartum), but the folic acid-supplemented group showed a more pronounced decrease in urine amylase activity than in the ethanol-fed group. At 30 days postpartum, no sex difference in urinary amylase was identified. However, in general, males showed higher values for urine amylase than females at 2 months postpartum. A folic acid-supplemented diet exerts an advantageous effect on amylase in serum in offspring males at 2 months postpartum of mothers fed ethanol during gestation and lactation periods, because amylase renal absorption is increased. In offspring females, amylase renal absorption is also increased, but we did not observed an advantageous effect on amylase in serum. It may be that sexual differentiation in females at 2 months postpartum exerts a definitive effect on amylase in serum. We found a sex-related difference in amylase activities; therefore, we suggest that in future all results of the exocrine pancreas function, in male and female animals, be analyzed separately.

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