Worthington Tissue Dissociation Guide
Dissociating Enzymes: Elastase
Pancreatic elastase is a serine protease with a specificity for peptide bonds adjacent to neutral amino acids. It also exhibits esterase and amidase activity. 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. It is produced in the pancreas as an inactive zymogen, proelastase, and activated in the duodenum by trypsin. Elastase is also found in blood components and bacteria.
Because elastin is found in highest concentrations in the elastic fibers of connective tissues, elastase is frequently used to dissociate tissues which contain extensive intercellular fiber networks. For this purpose, it is usually used with other enzymes such as collagenase, trypsin, and chymotrypsin. Elastase is the enzyme of choice for the isolation of Type II cells from the lung.
More Information: Worthington Elastase
Tissue Tables (references, grouped by tissue type and species)
Note: We have not limited the references listed to only those papers using Worthington enzymes. Generally speaking, the tissue dissociation enzymes offered by Worthington can be used interchangeably for most preparations cited.