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lipase

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lipase /lip·ase/ (li´pās) (lip´ās) any enzyme that catalyzes the cleavage of a fatty acid anion from a triglyceride or phospholipid.
lip·ase (lps, lps)
n.
Any of a group of lipolytic enzymes that cleave a fatty acid residue from the glycerol residue in a neutral fat or a phospholipid.

Lipase
A fat-splitting enzyme found in pancreatic juice, blood, and many tissues.
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lipase
[lī′pās, lip′ās]
Etymology: Gk, lipos, fat; Fr, diastase, enzyme
any of several enzymes produced by the organs of the digestive system that catalyze the breakdown of lipids through the hydrolysis of the linkages between fatty acids and glycerol in triglycerides and phospholipids. Normal blood levels of lipase range from 0 to 110 U/L. See also fat, fatty acid, glycerol, phospholipid, triglyceride.

lipase [li´pās, lip´ās]
fat-splitting enzyme; any enzyme that catalyzes the splitting of fats into glycerol and fatty acids. Measurement of the serum lipase level is an important diagnostic test for acute and chronic pancreatitis.

lipase,
n a fat-splitting or lipolytic enzyme.

lipase
fat-splitting enzyme; abbreviated LPS. Any enzyme that catalyzes the splitting of fats into glycerol and fatty acids. The two important sources in the body are the pancreas and the intestinal mucosa. Measurement of the serum levels of lipase is an important diagnostic test for acute and chronic pancreatitis. See also pancreatic lipase.

triglyceride lipase
see triacylglycerol lipase.

monoacylglycerol hydrolase, lipase
enzyme catalyzing the final hydrolytic removal of a fatty acid from monoacylglycerol releasing glycerol into the bloodstream; present in adipose tissue.


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Mayoly has succeeded in developing a recombinant Lipase (not of animal origin), an enzyme for the treatment of exocrine pancreatic insufficiency (EPI).
They found that moderate high pressures--between 150 MPa and 450 MPa--stabilize lipase activity in organic media, which allows processes to occur at temperatures higher that what is achievable at ambient pressure, because of enzyme denaturation and solvent evaporation.
During the study, the researchers looked at 585 subjects of European ancestry, and identified 10 people with previously unreported rare mutated forms of this gene that were unique to subjects with very high HDL-C levels Further analysis revealed that mutations in the LIPG gene that cause loss of endothelial lipase activity were the cause of increased plasma HDL-C levels.
 
 
 
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