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|Method & Line||Sample & Target||Product||Package Info||Product||Package Info|
|Clinical Chemistry||Serum||AMYLASE||Tests per Package: 683|
|Pchem Reagents||The Pchem Amylase Reagent Kit has been designed for use in the quantitative determination in vitro of the Amylase activity in human serum. The results of the test must always be interpreted in conjunction with the clinical picture.||Code: ADA-R0000000001||Package: R1 3 x 48.5 mL|
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The Pchem Amylase Reagent Kit has been designed for use in the quantitative determination in vitro of the Amylase activity in human serum. The results of the test must always be interpreted in conjunction with the clinical picture.
This kit is intended for In vitro diagnostic use only, must not be sold to the general public and the test has to be carried out by a health-care professional person.
The kit contains reagents sufficient for 683 tests.
For many years, the levels of serum and plasma a-amylase in patients have provided needed evidence for the diagnosis of the acute pancreatitis (1,3). Early assay techniques were based on either a change in the absorption maxima of the complex beaveen starch and iodine as the a-amylase degraded the starch; or a measurement of the increase in reducing groups as the starch was hydrolyzed by the a-amylase (4). These methods are not as reliable and easy to quantitative as spectrophotometric methods using a defined substrate (5). Some methods are based on the production of NADH proportionate to the activity of the a-amylase. A defined substrate, such as maltotetraose , is degraded by a-amylase to produce glucose which can be measured in a coupled enzyme assay. However, this method necessitates the removal of endogeneous glucose which would give a high background to the assay (5). More recent methods are based on the production of p-nitro-phenol from defined oligosaccharide substrates with blocking groups attached on the terminal sugar. The action of the a-amylase on the oligosaccharides yields a variety of chain lengths after hydrolysis. These methods then use a variety of coupling enzymes to hydrolyze the resulting short chain oligosaccharides to produce p-nitropheno (5). The coupling enzymes contain residual a-amylase activity that may significantly reduce the stability of the reagent.
The alpha-Amylase assay involves the use of a chromogenic substrate, 2-chloro-4-nitrophenol linked with maltotriose (7). Alpha-amylase hydrolyzes the 2-chloro-4-nitrophenyl-alpha-D-maltotrioside (CNPG3) to release 2-chloro-aminophenol (CNP) and form 2-chloro-4-nitrophenyl- α-D-maltoside (CNPG2), maltotriose (G3) and glucose (G). The rate of formation of the 2-chloro-4-nitrophenol can be detected spectrophotometrically at 405 nm to give a direct measurement of α-amylase activity in the sample. The reaction is not readily inhibited by endogeneous factors.
Pchem Amylase Reagent Kit
Reagent (R) – 3 x 48.5 mL/vial