CLINICAL CHEM 2 Day 3 1st Periodical PDF

Alpha-amylase (1,4-alpha-D-glucan glucanohydrolase) (GLYCOGENASE)  A digestive enzyme mainly secreted by the pancreatitis as well as the salivary glands and is used to digest carbohydrates in the gastrointestinal (GI) tract. Can be used to detect and monitor t...

Alpha-amylase (1,4-alpha-D-glucan glucanohydrolase) (GLYCOGENASE)  A digestive enzyme mainly secreted by the pancreatitis as well as the salivary glands and is used to digest carbohydrates in the gastrointestinal (GI) tract. Can be used to detect and monitor the clinical course of pancreatitis and usually precedes the lipase. It is frequently ordered when a patient presents with acute abdominal pain (especially epigastric pain that is described as radiating to the back and associated with nausea and vomiting). Aids in evaluation for disorders of GI tract, autoimmune and viral illnesses, shock, trauma, and  Adults = 60-120 Somogyi units/dL or 30-220 units/L (SI units) Newborn = 6-65 units/L. Level remains low for the first two months of life and increases to adult values by the end of the first year of life. Notes: Values may be slightly increased during normal pregnancy and in older adults. Critical values: > 3 x the upper limit of normal (ULN; depending on the method).  Pancreatitis: Amylase is normally secreted from pancreatic acinar cells into the pancreatic duct and then into the duodenum. Once in the intestine it aids in the catabolism of carbohydrates to their component simple sugars. Damage to pancreatic acinar cells causes an outpouring of this enzyme into the intrapancreatic lymph system and the free peritoneum. Blood vessels pick up the excess amylase. Lipase is an enzyme that breaks down triglycerides into free fatty acids and glycerol. Lipases are present in pancreatic secretions and are responsible for fat digestion. There are many different types of lipases; for example, hepatic lipases are in the liver, hormone- sensitive lipases are in adipocytes, lipoprotein lipase is in the vascular endothelial surface, and pancreatic lipase in the small intestine. The lipase group of enzymes is built on alpha and beta hydrolase folds. They work by employing chymotrypsin-like hydrolysis, which uses a histidine base, a serine nucleophile, and aspartic acid. Lipase is an enzyme that breaks down triglycerides into free fatty acids and glycerol. Lipases are present in pancreatic secretions and are responsible for fat digestion. Lipases are enzymes that play a crucial role in lipid transport. There are many different types of lipases; hepatic lipases are in the liver, hormone-sensitive lipases are in adipocytes, lipoprotein lipase is in the vascular endothelial surface, and pancreatic lipase is in the small intestine, each serving individual functions. Hepatic lipase plays a crucial role in the formation and delivery of low-density lipoprotein(LDL). LDL is formed by the modification of intermediate density lipoprotein in the peripheral tissue and liver by hepatic lipase. These LDL particles are taken up, or endocytosed, via receptor-mediated endocytosis by target cell tissue. LDL serves to ultimately transport cholesterol from the liver to peripheral tissue An enzymatic, kinetic method for determining serum lipase activity was evaluated and compared. The kinetic method was a commercial kit adapted for use on a tandem access clinical chemistry analyzer and utilized a series of coupled enzymatic reactions based on the hydrolysis of 1,2- diglyceride by lipase The manual method was the Cherry-Crandall technique based on the titration of base against the acid formed by hydrolysis of an olive oil substrate by lipase. Hydrolysis of triglycerides is catalyzed by lipase to produce glycerol and free fatty acids. The glycerol generated is then phosphorylated by adenosine 5'-triphosphate in the presence of glycerol kinase. Oxidation of the resulting glycerol 3-phosphate to produce hydrogen peroxide is catalyzed by L- alpha-glycerophosphate oxidase. An intense red chromogen is produced by the peroxidase-catalyzed coupling of 4- aminoantipyrene and sodium 2-hydroxy-3,5- dichlorobenzenesulfonate with hydrogen The method1,2 is based on the hydrolysis of α- naphtyl phosphate at pH 5.0 by acid phosphatase (ACP) to produce α-naphtol and inorganic phosphate. The pentanediol acts as a phosphate acceptor increasing the reaction sensitivity. The α- naphtol reacts with Fast Red TR* , to produce a coloured complex directly proportional to the activity of the ACP in the sample. α-Naphtyl phosphate + H2O---------ACP----- α-Naphtol + Pi α-Naphtol + Fast Red TR----PH 5 30 C------------- Azo dye Diazotized 2- Amino-5-chlorotoluene The sample tested in the presence of L-tartrate inhibits the prostatic acid phosphatase of the total ACP activity.