Dispase

Dispase is a non-specific protease derived from the bacterium Bacillus polymyxa. It is used in the laboratory for cell dissociation, as it cleaves the peptide bonds in collagen.

History

Dispase was first isolated from Bacillus polymyxa in the 1970s. It was found to have proteolytic activity, specifically against collagen, and has since been used in various biological and medical research applications.

Structure and Function

Dispase is a serine protease, meaning it has a serine residue in its active site that is crucial for its enzymatic activity. It cleaves peptide bonds in collagen, a major component of the extracellular matrix that provides structural support to cells. By breaking down collagen, dispase can dissociate cells from each other and from their substrate.

Applications

Dispase is widely used in the laboratory for cell dissociation. It is particularly useful for isolating individual cells from tissue or cell clusters for further study. Dispase is also used in the preparation of single cell suspensions for flow cytometry, a technique used to analyze the physical and chemical characteristics of cells or particles in a fluid.

In addition to its use in cell dissociation, dispase has been used in the clinic for the treatment of certain skin conditions. For example, it has been used to remove the outer layer of skin in patients with severe burns to facilitate skin grafting.

Safety and Precautions

While dispase is generally safe to use in the laboratory, precautions should be taken to avoid inhalation, ingestion, or contact with skin or eyes. It is recommended to use personal protective equipment, such as gloves and safety glasses, when handling dispase.

See Also

• Collagenase
• Trypsin
• Elastase

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