Clostridiopeptidase

Clostridiopeptidase (also known as Collagenase Clostridium histolyticum) is a bacterial enzyme produced by the bacteria Clostridium histolyticum. This enzyme is used in medical applications due to its ability to break down collagen, a protein that forms the framework of connective tissue in animals.

History

The discovery of clostridiopeptidase dates back to the 1950s when researchers identified the collagen-digesting ability of Clostridium histolyticum. The enzyme was later isolated and named clostridiopeptidase.

Structure

Clostridiopeptidase is a protein composed of several polypeptide chains. The enzyme's structure allows it to bind to collagen and break it down into smaller peptides.

Function

The primary function of clostridiopeptidase is to degrade collagen, a major component of connective tissue. This function is utilized in medical treatments, such as the management of Dupuytren's contracture, a condition characterized by the abnormal thickening of the connective tissue in the hand.

Medical Applications

Clostridiopeptidase is used in the treatment of several medical conditions that involve excess collagen. These include Dupuytren's contracture, Peyronie's disease, and fibrosis. The enzyme is administered through injection, where it works to break down the excess collagen and improve the condition's symptoms.

Side Effects

Like all medications, clostridiopeptidase can cause side effects. These may include swelling, bruising, and bleeding at the injection site. More serious side effects can occur if the enzyme is administered incorrectly or in too high a dose.

See Also

• Collagenase
• Clostridium histolyticum
• Dupuytren's contracture
• Peyronie's disease
• Fibrosis

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