Liquimax Amylase SLR

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-αglucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose. 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 there fore organ specific, The S-type can originate from a number of sites. Apart from 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-á-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 enzymecatalyzed subsequent reactions.The kinetic method described here is based on the cleavage of 2-chloro-4-nitrophenyl-α- D-maltotrioside (CNP-G3) by α-amylase