Colipase from porcine pancreas

Colipase from porcine pancreas has been used:

• in the enzyme solution for lipase assay
• in an enzyme mixture to simulate gastrointestinal digestion
• as one of the apparent critical factors to study its effect on lycopene in vitro accessibility

Colipase is involved in lipid metabolism and apoptosis signaling. It is crucial for fat digestion. It is a pancreatic protein that prevents the denaturation of lipase and enables its attachment to the lipid-water interphase of the droplet. Colipase makes lipase accessible to the inner core of triacylglycerol. Defective colipase secretion induced by an insufficient exocrine pancreatic function minimizes the luminal hydrolysis of dietary fat. Lack of congenital lipase or colipase causes pancreatic fat malabsorption.

Colipase, a small protein cofactor, is essential for efficient dietary lipid hydrolysis by pancreatic lipase. It attaches to the non-catalytic C-terminal domain of the lipase, stabilizing an active conformation and significantly enhancing the overall hydrophobic binding site. This pancreatic exocrine protein aids in the adsorption of pancreatic triglyceride lipase (PTL) to the substrate lipid-water interface.

Research Area: Cell Signaling
Colipase is a member of a group of small cysteine-rich proteins characterized by a limited secondary structure. Its structure is relatively flat, measuring 25×30×35 Å, resembling an arrangement of protruding fingers interconnected at one end by a complex network of five disulfide bridges. The colipase structure comprises two small domains with closely related topology.

The gene colipase (CLPS) encodes a lipolytic enzyme that is majorly expressed in the exocrine pancreas. This protein is also found in the stomach and intestine. Its structure includes 17 amino acid signal peptides and a five amino acid pro-piece at the N-terminus.

Dissolves in water to form a clear, colorless to faint yellow colored solution at 1.9-2.1 mg/mL concentration.