Use of Serum Amylase Isoenzymes in Evaluation of Pancreatic Function

PEDIATRICS ◽  
1974 ◽  
Vol 54 (2) ◽  
pp. 229-235
Author(s):  
Lynn M. Taussig ◽  
Robert O. Wolf ◽  
Robert E. Woods ◽  
Richard J. Deckelbaum
Keyword(s):  
Enzyme Activities ◽  
Serum Amylase ◽  
Pancreatic Enzyme ◽  
Normal Subjects ◽  
Normal Serum ◽  
Pancreatic Function ◽  
Total Serum ◽  
Duodenal Fluid ◽  
Pancreatic Isoamylase ◽  
Amylase Isoenzymes

Amylase isoenzyme patterns were evaluated in serum, urine, and duodenal fluid from 19 patients with cystic fibrosis (CF) and normal subjects. Two thirds of the CF patients with absent pancreatic enzymes lacked a serum pancreatic isoamylase band, while the remainder had a markedly diminished pancreatic band when compared to the salivary isoamylase. In normal sera the pancreatic band is equal to or greater than the salivary band. In all patients with absent enzymes the diagnosis of abnormal pancreatic function could have been made by evaluation of serum isoamylase patterns thereby avoiding duodenal intubation or collection of 72-hour stools for proteolytic enzyme activities. The patients with normal pancreatic enzyme activities had normal serum zymograms. No CF patient had a low total serum amylase concentration. Total duodenal fluid amylase levels may be misleading in the evaluation of pancreatic function since the amylase may be of salivary origin. The advantages of this isoamylase method include (1) simplicity and noninvasiveness, requiring only a small blood sample; (2) specificity for pancreatic function; and (3) independence of pancreatic enzyme medication.

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.

Investigation of Serum Lipoproteins and Apoproteins in Abetalipoproteinaemia

1974 ◽  
Vol 46 (4) ◽  
pp. 457-468
Author(s):  
G. Kostner ◽  
A. Holasek ◽  
H. G. Bohlmann ◽  
H. Thiede
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Cholesterol Acyltransferase ◽  
Normal Subjects ◽  
Normal Serum ◽  
High Density ◽  
High Density Lipoproteins ◽  
Total Serum ◽  
Serum Lipoproteins ◽  
Acyltransferase Activity ◽  
Lecithin Cholesterol Acyltransferase

1. The serum lipoproteins, apoproteins and lecithin—cholesterol acyltransferase activity of three patients with abetalipoproteinaemia have been studied. 2. Concentration of lipoproteins with a density of less than 1·063 was found to be 5–6 mg/100 ml of plasma. The protein part consisted only of apoAI polypeptides. 3. Concentration of total serum high-density lipoproteins was 90–100 mg/100 ml. After total delipidization of this fraction, apoproteins were separated by column chromatography. All apoA and most of the apoC peptides could be demonstrated by immunochemical methods and polyacrylamide gel electrophoresis. 4. Quantification of individual polypeptides indicated that the proportions apoAI: apoAII: apoAIII in high-density lipoproteins were not different from those observed in normal subjects. ApoCIII1 was absent in the patients' serum. In the remaining apoC peptides differences in the distribution compared with normal subjects could be demonstrated. 5. With antibodies to lipoprotein B, acetylated lipoprotein B or apolipoprotein B no reaction could be observed with abetalipoproteinaemic serum or any density fraction tested including density 1·23 infranate. 6. Isoelectric focussing of prestained lipoproteins in complete patients' serum revealed the absence of four major lipoprotein families present in normal serum. 7. Lecithin—cholesterol acyltransferase activity of abetalipoproteinaemic serum was reduced to a value of about 50% of normal but lipoproteins of patients' serum could be utilized as a substrate only to a minor degree. The maximum activity was observed only if lipoproteins of normal serum were added to the assay system.

Serum Amylases, Isoenzymes, and Pancreatitis I. Effect of Substrate Variation

1968 ◽  
Vol 14 (12) ◽  
pp. 1176-1184 ◽  
Author(s):  
Samuel Meites ◽  
Saul Rogols
Keyword(s):  
Serum Amylase ◽  
Corn Starch ◽  
Potato Starch ◽  
Normal Serum ◽  
Duodenal Fluid ◽  
Waxy Maize ◽  
Organ Specific ◽  
Substrate Variation ◽  
High Amylose ◽  
Pancreatic Extract

Abstract Four plant starches were used to study human amylase activity in normal serum and urine, "pancreatitis" serum, duodenal fluid (secretin stimulated), saliva, and pancreatic extract. The starches were derived from waxy maize, high amylose corn, potato, and corn (pearl), and were lintnerized. It was shown that the rate of digestion of starch by each of the fluids tested depends on the plant starch selected as substrate. Digestion of waxy maize was most rapid. The advantages of using waxy maize as a substrate are indicated as a means of markedly enhancing the sensitivity of serum amylase determination. It was also found that normal serum, urine, and saliva digested potato starch at a greater rate than corn starch with few exceptions, while pancreatitis serum, secretin-stimulated duodenal fluid, and pancreatic extract digested corn starch at a greater rate than potato. These findings suggest that organ-specific amylases exist, and that plant starches might be used to distinguish them.

In vitro Inhibition of Pancreatic Enzyme Activities by Dietary Fiber

Digestion ◽  
1982 ◽  
Vol 24 (1) ◽  
pp. 54-59 ◽  
Author(s):  
G. Isaksson ◽  
I. Lundquist ◽  
I. Ihse
Keyword(s):  
Dietary Fiber ◽  
Enzyme Activities ◽  
Pancreatic Enzyme ◽  
In Vitro Inhibition

Survival of human pancreatic enzymes during small bowel transit: effect of nutrients, bile acids, and enzymes

1997 ◽  
Vol 273 (2) ◽  
pp. G553-G558 ◽  
Author(s):  
G. Holtmann ◽  
D. G. Kelly ◽  
B. Sternby ◽  
E. P. DiMagno
Keyword(s):  
Bile Acids ◽  
Enzyme Activities ◽  
Lipolytic Activity ◽  
Pancreatic Enzyme ◽  
Pancreatic Enzymes ◽  
Intestinal Transit ◽  
Small Bowel Transit ◽  
Healthy Humans ◽  
Proximal Intestine ◽  
Distal Jejunum

The activity of pancreatic enzymes declines during aboral intestinal transit. We tested the hypothesis that survival of pancreatic enzyme activities during intestinal transit is affected by amounts or concentrations of calories, nutrients, bile acids, or pancreatic enzymes entering the segments of the small intestine. An oroileal tube was placed in 26 healthy humans. The tube had duodenal, jejunal, and ileal infusion ports for nonabsorbable markers and aspiration ports in the distal duodenum, distal jejunum, and distal ileum. Four infusates of different proportions of protein, fat, and carbohydrate were infused continuously into the duodenum at 40, 90, and 160 kcal/h. Of the nutrients infused into the proximal duodenum, 21 +/- 3, 51 +/- 7, and 39 +/- 5% of fat, protein, and carbohydrate, respectively, were delivered to the distal duodenum. During duodenoileal transit, lipase, chymotrypsin, amylase, and trypsin lost 71 +/- 5, 63 +/- 5, 43 +/- 7, and 38 +/- 9% of activity, respectively (P < 0.01 vs. distal duodenum). During duodenojejunal transit, the activity of each enzyme decreased more than 35% (P < 0.01 vs. distal duodenum), and infusion of more calories into the duodenum improved survival of all enzymes except trypsin (P < 0.05). During jejunoileal transit, greater amounts and concentrations of calories and carbohydrate improved survival of only lipolytic activity (P < 0.01, P < 0.05, respectively), and loss of lipolytic activity correlated directly with delivery of bile acids (r = 0.56, P = 0.05) and chymotrypsin (r = 0.80, P = 0.001) to the distal jejunum. We conclude that intraluminal nutrients increase survival of enzyme activities in the proximal intestine. After absorption of nutrients, the action of chymotrypsin and bile acids decrease lipolytic activity more than activity of other enzymes.

Gastric and Pancreatic Enzyme Activities and their Relationship with Some Gut Regulatory Peptides during Postnatal Development and Weaning in Calves

1992 ◽  
Vol 122 (7) ◽  
pp. 1434-1445 ◽  
Author(s):  
Isabelle Le Huerou-Luron ◽  
Paul Guilloteau ◽  
Catherine Wicker-Planquart ◽  
Jean-Alain Chayvialle ◽  
John Burton ◽  
...  
Keyword(s):  
Postnatal Development ◽  
Enzyme Activities ◽  
Pancreatic Enzyme ◽  
Regulatory Peptides

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.

STUDIES OF FIBROCYSTIC DISEASE OF THE PANCREAS (MUCOVISCIDOSIS): CHYMOTRYPSIN ACTIVITY OF DUODENAL FLUID

PEDIATRICS ◽  
1955 ◽  
Vol 16 (2) ◽  
pp. 207-214
Author(s):  
Reid C. Richmond ◽  
Harry Shwachman
Keyword(s):  
Respiratory Infections ◽  
Pancreatic Insufficiency ◽  
Pancreatic Function ◽  
Control Group ◽  
Fibrocystic Disease ◽  
Complete Evaluation ◽  
Total Enzyme Activity ◽  
Duodenal Fluid ◽  
Chymotrypsin Activity ◽  
Routine Assay

A study of the chymotrypsin activity of duodenal fluid, using the method of Ravin, Bernstein, and Seligman, is presented. The method is applicable to routine assay and is a reliable reflection of pancreatic function. In addition, this assay is specific for chymotrypsin activity in contrast to the customary tests for protease activity, which use casein or gelatin as substrates. In 40 patients with complete pancreatic insufficiency due to fibrocystic disease of the pancreas the chymotrypsin activity of the duodenal fluid was not measurable (i.e., less than 5 µg. of β-naphthol liberated from the substrate). The chymotrypsin activity in 53 patients with normal pancreatic function and without symptoms referable to fibrocystic disease of the pancreas varied from 11 to 65 µg. of βd-naphthol except for the lowest value in this control group of 8 µg. In another group of 62 children with sufficient symptoms to call for duodenal fluid assay (failure to gain, abnormal feces or repeated respiratory infections) the range of chymotrypsin activity was similar to that of the control group. The duodenal fluid assay and clinical course excluded fibrocystic disease of the pancreas in this group. The chymotrypsin assay is useful in the study of patients with partial pancreatic insufficiency from progressive loss of pancreatic function as the disease progresses. In view of occasional diagnostic failures, based on assay of a single enzyme, it is important to determine the total enzyme activity of duodenal fluid for proper complete evaluation of pancreatic function.

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