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[Proteolytic complex from Aspergillus terricola (review)]
Prikladnaia Biokhimiia I Mikrobiologiia
|January 1, 1986
Summary
This study details Terrilytin, an anti-inflammatory drug derived from Aspergillus terricola. It comprises three serine and metalloproteases, demonstrating fibrinolytic activity by hydrolyzing fibrin and fibrinogen.
Area of Science:
- Biochemistry
- Enzymology
- Pharmacology
Background:
- Terrilytin is an anti-inflammatory drug derived from the fungus Aspergillus terricola.
- The drug's composition and enzymatic properties were previously not fully elucidated.
Purpose of the Study:
- To characterize the proteolytic enzymes within Terrilytin.
- To understand the enzymatic basis of Terrilytin's anti-inflammatory and fibrinolytic activities.
Main Methods:
- Physico-chemical characterization of isolated enzymes.
- Enzymatic assays to determine protease types and activity.
- Analysis of enzyme interactions with fibrin and fibrinogen.
Main Results:
- Terrilytin is a complex of three proteolytic enzymes and amylase.
- Two proteases (I and II) are serine proteases; Protease III is a zinc-dependent metalloprotease.
- All three proteases exhibit fibrinolytic activity by hydrolyzing fibrin and fibrinogen.
Conclusions:
- Terrilytin's therapeutic effects are attributed to its complex enzymatic profile.
- The identified serine and metalloproteases are key to its fibrinolytic action.
- Further research into microbial metalloproteases and serine proteases is warranted.