Elastase

Porcine pancreatic elastase has a molecular weight of 25.9 kDa, and a pH optimum of 8.5.  While elastase will hydrolyze a wide variety of protein substrates, it is unique among proteases in its ability to hydrolyze native elastin, a substrate not attacked by trypsin, chymotrypsin or pepsin. Soybean trypsin inhibitor and kallikrein inhibitor suppress proteolytic but not elastolytic activity.  Elastase is assayed using a method adapted from that of Feinstein et al., Biochem. Biophys. Res. Comm., 50, 1020 (1973) and using the more soluble substrate of Bieth et al., Biochem. Med., 11, 350 (1974).

Purified:

• ≥8 units per mg protein
• Chromatographically purified. A lyophilized powder.

Lyophilized:

• ≥3 units per mg protein
• 2X Crystallized
• Supplied as a dialyzed, lyophilized powder.
• The enzyme should be 0.22 micron filtered after reconstitution and prior to use.
• Suitable for the isolation of Type II lung cells.

Suspension:

• ≥3 units per mg protein
• 2X crystallized
• Supplied as an aqueous suspension. Due to viscosity container should be rinsed.
• This preparation must be diluted to dissolve the enzyme.
• The diluted enzyme should be 0.22 micron filtered before use.
• Suitable for the isolation of Type II lung cells.

One Unit cleaves one micromole of N-succinyl-L-alanyl-L-alanyl-L-alanine-p-nitroanilide per minute at 25°C, pH 8.0.

1 SucAla₃NA unit is approximately equivalent to 6 elastin digestion units.

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