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Pancreatic Amylase IFCC EPS-G7-Substrate


Pancreatic Amylase IFCC EPS-G7-Substrate
The Alpha-amylases (1.4-Alpha-D-glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1.4-a-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 a-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, Alpha -amylase determinations are of considerable importance in pancreatic diagnostics. The determination of pancreas-specific a-amylase instead of total -a-amylase is of advantage here.

The determination of pancreatic a-amylase is suitable for the diagnosis and monitoring of acute pancreatitis and acute attacks during chronic pancreatitis. In terms of clinical sensitivity and specificity, the diagnostic value of pancreatic-Alpha-amylase is comparable to that of lipase, the generally recognized pancreas-specific enzyme. The sensitivity of pancreatic Alpha-amylase is 38% higher than that of total Alpha-amylase in the diagnosis of acute pancreatitis when - as commonly used - three times the upper normal limit is taken as the criterion. A variety of methods have been described for determining pancreatic Alpha-amylase: radio- and enzyme-immunoassays as well as the partial inhibition of salivary a-amylase by an inhibitor derived from wheatgerm and calculation of the pancreatic a-amylase from the remaining and total amylase activities.

The kinetic method described here is based on inhibition of the activity of human salivary a-amylase by two different monoclonal antibodies and the well-proven cleavage of 4.6-ethylidene-(G7)-1.4-nitrophenyl-(G1)-a1D-maltoheptaoside (Ethylidene Protected Substrate = EPS) by pancreatic -Alpha.-amylase followed by hydrolysis of all the degradation products to p-nitrophenol with the aid of a-glucosidase (100% chromophore liberation). The results of this method correlate with those obtained by HPLC.

Intended use
Enzymatic in vitro test for the quantitative determination of pancreatic Alpha-amylase in human serum, plasma and urine.

Test principle
Enzymatic colorimetric assay, according to the IFCC method for total amylase.

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