Labkit Amylase- LQ Biochemistry Reagent

α-Amylases split the α-1,4 glycosidic linkages in amylase to yield maltose and glucose, but they do not act on maltose, a disaccharide composed of two glucose subunits linked by an α-1,4 linkage.

In theory α-amylase will ultimately degrade a solution of amylase to maltose, and glucose which can be released from the ends of the chains. Salivary amylase starts the digestion of starch. It continues to act for up to half an hour in the interior of the food bolus after it has arrived in the stomach.

It is eventually inactivated at the low pH produced by the gastric acid when it penetrates the food bolus. It can digest up to 50% of the starch present in food. Pancreatic juice that contains a second α-amylase is released into the duodenum when a meal is present in the digestive tract. Pancreatic amylase continues the digestion of starch and glycogen in the small intestine. It is produced in larger amounts than salivary amylase.

The α-amylases from the two sources have similar catalytic properties, despite having different amino acid sequences. They both require Cl⁻ for optimum activity and both act at neutral or slightly alkaline pH values.

Analysis of serum amylase is mainly used in the diagnosis of the pancreatic diseases (acute or chronic pancreatitis and their complications, carcinoma).

During acute pancreatitis, a transitory increase of serum amylase is observed, a peak being reached approximately 12h after the beginning, the activity returning to the normal after 3 or 4 days. However, a serum amylase increase is also observed in other intra-abdominal pathologies, ovary or lung cancers, salivary gland lesions, acute alcoholism, renal insufficiency ormacroamylasemia (presence of a complex amylase-IgG not filtered by theglomerulus).