Colipase pancreatic lipase when prepared essentially free of co-lipase is strongly inhibited by conjugated bile salts at or above their critical micell concentration. Addition of co-lipase restores activity to the bile-salt-inhibited lipase and gelfilteration experiments indicate that co-lipase in bile salt solution makes a dimer which forms a 1:1 complex with lipase (Morgan, R.G., and N.E. Hoffman, Biochim Biophys Acta, 248, 143-148, 1971). Lipase and co-lipase interact as a stoichiometrical relationship and classified co-lipase interact as a co-enzyme for lipase. The co-lipase is a single chain polypeptide with a molecular weight approximately 11,000 with 5 disulfide bridges and isoelectric point 5.0. (Mayie, M.E., et al, Biochim Biophys Acta, 271, 400-412, 1971).

Source:
Native porcine pancreas

Molecular Weight:
~11kD

Protein:
≥95%

Form:
Lyophilized powder

Activity:
4000-12,000U/mg

Specific Activity:
As Reported

Unit Definition:
The amount of enzyme causing the release of one micromole of fatty acid from tributyrin per minute at 25°C..

Solubility:
Water or dilute buffer

Storage and Stability:
Lyophilized and reconstituted products are stable for 6 months after receipt at -20°C. Reconstitute with sterile ddH2O or buffer. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.