Early and Sustained Elevation in Serum Pancreatic Amylase Activity

2021 ◽  
Vol Publish Ahead of Print ◽  
Author(s):  
Elisa Bannone ◽  
Giovanni Marchegiani ◽  
Alberto Balduzzi ◽  
Giuseppa Procida ◽  
Pier Giuseppe Vacca ◽  
...  
Keyword(s):  
Amylase Activity ◽  
Pancreatic Amylase

Rapid quantitative, specific measurement of pancreatic amylase in serum with use of a monoclonal antibody.

1985 ◽  
Vol 31 (8) ◽  
pp. 1283-1286 ◽  
Author(s):  
T E Mifflin ◽  
D C Benjamin ◽  
D E Bruns
Keyword(s):  
Polyvinylidene Fluoride ◽  
Amylase Activity ◽  
Kinetic Method ◽  
Reference Intervals ◽  
Pancreatic Amylase ◽  
Salivary Amylase ◽  
Electrophoretic Method ◽  
Standard Curve ◽  
A Value ◽  
Analytical Recovery

Abstract In this rapid quantitative assay for pancreatic alpha-amylase (EC 3.2.1.1) in serum, we precipitate salivary amylases by 10-min incubation with monoclonal anti-salivary amylase antibody immobilized on particles of polyvinylidene fluoride. We then centrifuge the serum mixture and measure the pancreatic amylase activity remaining in the supernate by a kinetic method. The assay requires 50 microL of serum and the standard curve is linear to at least 1300 U of pancreatic amylase per liter of serum. CVs were 1.3% within-run, 6-8% day-to-day. Apparent analytical recovery of pancreatic amylase activity added to serum was 101% +/- 2%. Addition of purified salivary amylase, 356 U/L, to sera gave a value for apparent pancreatic amylase of less than 4 U/L, or 1% of the added salivary amylase activity. This assay correlated well with an electrophoretic method (slope, 0.97-0.99; intercept, 0.5 to -4 U/L; correlation coefficient, 0.946-0.990; and standard error of the estimate 3-5 U/L). Estimated normal reference intervals with maltotetraose as substrate were: total amylase, 39-118 U/L; pancreatic amylase, 11-50 U/L; and salivary amylase, 18-79 U/L.

THE EFFECT OF THYROID ADMINISTRATION ON THE PANCREATIC AMYLASE ACTIVITY OF HYPOPHYSECTOMIZED AND INTACT RATS

1963 ◽  
Vol 41 (6) ◽  
pp. 1373-1379 ◽  
Author(s):  
Madelaine O. Maykut ◽  
Margaret T. Nishikawara ◽  
R. E. Haist
Keyword(s):  
Body Weight ◽  
Thyroid Gland ◽  
Amylase Activity ◽  
Total Activity ◽  
Pancreatic Amylase ◽  
Hypophysectomized Rats ◽  
Dose Levels ◽  
Marked Atrophy ◽  
Intact Rats

The administration of desiccated thyroid gland to hypophysectomized rats prevented the marked atrophy of the pancreas which was consistently observed following hypophysectomy. Thyroid feeding at two dose levels led to a significant increase in the pancreatic amylase activity of hypophysectomized rats. This held whether the results were expressed as total activity or were given as activity per unit of body weight, per unit of pancreas, or per mg nitrogen. Except for the activity per unit of body weight, the amylase activity of the thyroid-treated hypophysectomized rats was significantly lower than the amylase activity in untreated, intact controls. In the thyroid-fed, hypophysectomized rats the amylase activity per unit of body weight was not significantly different from that of intact, untreated controls.Thyroid administration in intact rats resulted in a decrease in the pancreatic amylase activity.

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.

THE EFFECTS OF TEMPERATURE UPON PANCREATIC AMYLASE IN SELECTED REPTILES AND AN AMPHIBIAN

1967 ◽  
Vol 45 (2) ◽  
pp. 227-232 ◽  
Author(s):  
Yvette Abrahamson ◽  
Michael Maher
Keyword(s):  
Thermal Stability ◽  
Amylase Activity ◽  
Effect Of Temperature ◽  
Maximum Temperature ◽  
Pancreatic Amylase ◽  
Optimum Temperature ◽  
Preferred Temperatures ◽  
Effects Of Temperature ◽  
Subcellular Level ◽  
Thermal Stability Of

The effect of temperature on pancreatic amylase was studied on three species of reptiles and one amphibian. Pancreata were removed from the animals, homogenized, and assayed for amylase activity by the Caraway procedure. Assays were conducted at various temperatures to determine the optimum temperature of activity and the maximum temperature for thermal stability of pancreatic amylase. It appears that between reptiles and amphibians, and also among species of reptiles, there are thermally dependent differences at the subcellular level which are similar to the differences in the preferred temperatures of the animals.

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.

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.

Crucial role of milk-borne insulin in the development of pancreatic amylase at the onset of weaning in rats

1998 ◽  
Vol 275 (6) ◽  
pp. R1958-R1967 ◽  
Author(s):  
Toshi Kinouchi ◽  
Kyoko Koizumi ◽  
Tamotsu Kuwata ◽  
Takaji Yajima
Keyword(s):  
Plasma Concentration ◽  
Amylase Activity ◽  
Milk Formula ◽  
Immunoreactive Insulin ◽  
Pancreatic Amylase ◽  
Plasma Insulin Concentration ◽  
Physiological Concentration ◽  
Rat Pups ◽  
Endogenous Insulin ◽  
Old Rats

The development of pancreatic amylase activity was examined in rats fed in regular cages or in special cages, designed so the pups could not reach solid food to prevent weaning. In both groups, the amylase activity in zymogen granules increased in rat pups aged 14 days, peaked at 18 days, and thereafter remained at a 1.6-fold higher level than at 14 days of age. An increase in the plasma concentration of immunoreactive insulin preceded the increase of amylase activity, whereas the plasma concentration of C-peptide, indicating the secretion rate of endogenous insulin, remained unchanged. The administration of insulin at 20 ng/ml (the physiological concentration) in the milk formula caused an increase in the plasma insulin concentration of 17-day-old pups. In addition, increased pancreatic amylase activity was observed in 17-day-old rats raised on milk formula to which insulin was added. We propose that the increase of amylase activity at the beginning of weaning is dependent on the milk-borne insulin and not on the dietary change in rats.

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