Purification and Characterization of a Fibrinolytic Enzyme from Snake Venom of Macrovipera Lebetina Turanica

(6) Journal of Pharmacopuncture, Vol 14, No. 2, pp. 5–14, 2011

Purification and Characterization of a Fibrinolytic Enzyme from Snake Venom of Macrovipera Lebetina Turanica

Ki-Rok Kwon, Do-Il Park, Seung-Bae Lee, Suk-Ho Choi

Abstract

Objectives: In this research fibrinolytic enzyme preparations were isolated from the snake venom of Macrovipera lebetica turanica.

Methods: The purity of the preparations was determined using SDS-PAGE and the enzymic characteristics of the purified fibrinolytic enzyme were determined.

Results:

• 1. Two preparations with fibrinolytic activity obtained from the snake venom of M. l. turanica contained a major polypeptide with a molecular weight of 27,500. One of the preparations showed purified fibrinolytic enzyme.

• 2. The purified fibrinolytic enzyme hydrolyzed the α-chain of fibrinogen faster than the β-chain, but did not hydrolyze the γ-chain.

• 3. The fibrinolytic activity was inhibited completely by EDTA, EGTA, 1–10-phenanthroline, and dithiothreitol.

• 4. The fibrinolytic activity was inhibited completely by calcium chloride, iron(III) chloride, mercuric chloride, and cobalt (II) chloride.

• 5. The fibrinolysis zone formed after addition of zinc sulfate was smaller, but clearer, it was for than the control.

Conclusions: These results suggest that the fibrinolytic enzyme purifed from the snake venom of M. l turanica was a metalloprotease containing a dithiol group.

Key Words: snake venom; Macrovipera lebetica turanica; fibrinolytic enzyme, Fibrinolytic activity