BIOCHEMISTRY - Textbook - Ostapchenko L. I. - 2012

Chapter 7. ENZYMOLOGY

7.9. Application of Enzymes in Medicine

7.9.2. Enzymes as Medicinal Products

The Application of Enzymes as therapeutic agents faces many limitations due to their high immunogenicity. Despite this, enzyme therapy is actively developing in the following directions:

✵ replacement therapy - The use of enzymes to compensate for their deficiency;

✵ elements of combination therapy - the use of enzymes in conjunction with other therapeutic agents.

Replacement enzymotherapy is effective for gastrointestinal disorders associated with insufficient secretion of digestive juices. For example, Pepsin is used in achylia, hypoacid and anacid gastritis. Pancreatic enzyme deficiency can also be largely compensated for by taking medications containing key pancreatic enzymes (Festal, Enzistal, Mezim-forte, etc.).

As complementary therapeutic agents, enzymes are used in the Treatment of various diseases. Proteolytic Enzymes (Trypsin, Chymotrypsin) are applied topically for treating purulent wounds to break down Proteins from necrotic Cells, as well as for removing Blood clots or viscous secretions during inflammatory respiratory diseases. The enzyme preparations Ribonuclease and deoxyribonuclease are used as antiviral agents in the treatment of adenoviral Conjunctivitis and herpetic keratitis.

Enzyme preparations have become widely used in the treatment of thrombosis and thromboembolism. For this purpose, preparations of fibrinolysin, streptolyase, streptodecase, and urokinase are employed. Hyaluronidase (lidase), which catalyzes the degradation of hyaluronic acid, is administered either subcutaneously or intramuscularly to promote the resorption of scar contractures following Burns and surgeries (hyaluronic acid forms cross-links in Connective Tissue).

Enzyme preparations are also utilized in oncology. For instance, asparaginase, which catalyzes the catabolic reaction of asparagine, is used in the treatment of leukemias:

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The rationale behind the antileukemic effect of asparaginase was the discovery in leukemic cells of a defective asparagine synthetase enzyme, which catalyzes the synthesis of asparagine:

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Leukemic cells are unable to synthesize asparagine and must obtain it from Blood Plasma. If the asparagine present in blood plasma is degraded by administering asparaginase, the leukemic cells experience an asparagine deficiency, leading consequently to the disruption of cellular METABOLISM.



Last update: 06/08/2026

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