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Amylase, Body Fluid
MessagePerformed at SQL - 2060
Performed in Chemistry for BUMCT, Wyoming Medical Center.
BUMCT performs for BUMCS.
Wyoming Medical Center performs for PCMH, WMC and TCH.
Performed in Chemistry for BUMCT, Wyoming Medical Center.
BUMCT performs for BUMCS.
Wyoming Medical Center performs for PCMH, WMC and TCH.
Test Code
AMYLBF
Preferred Specimen
Fluid
FDA Status
FDA Approved
Setup Schedule
Daily, Sunday through Saturday
Report Available
Less than 4 hours
Reference Range
Performance characteristics for this test have been evaluated and verified by the laboratory. There is no established reference range for body fluids. Test results must be interpreted within the clinical context.
Clinical Significance
The α‑amylases (1,4‑α ‑D‑glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1,4‑α ‑glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of α ‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ‑specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube.
Because of the sparsity of specific clinical symptoms of pancreatic diseases, α ‑ amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas‑specific enzyme ‑ lipase or pancreatic‑α ‑amylase ‑ also be determined.
Numerous methods have been described for the determination of α ‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme‑ catalyzed subsequent reactions. The kinetic method described here is based on the well‑proven cleavage of 4,6‑ethylidene‑(G7)‑1,4‑nitrophenyl‑(G1)‑ α,D‑ maltoheptaoside (Ethylidene Protected Substrate = EPS) by α ‑amylase and subsequent hydrolysis of all the degradation products to p‑nitrophenol with the aid of α ‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC.
Because of the sparsity of specific clinical symptoms of pancreatic diseases, α ‑ amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas‑specific enzyme ‑ lipase or pancreatic‑α ‑amylase ‑ also be determined.
Numerous methods have been described for the determination of α ‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme‑ catalyzed subsequent reactions. The kinetic method described here is based on the well‑proven cleavage of 4,6‑ethylidene‑(G7)‑1,4‑nitrophenyl‑(G1)‑ α,D‑ maltoheptaoside (Ethylidene Protected Substrate = EPS) by α ‑amylase and subsequent hydrolysis of all the degradation products to p‑nitrophenol with the aid of α ‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC.
Additional Information
Amylase, Body Fluid
