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KMID : 0613820100200060838
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Journal of Life Science
2010 Volume.20 No. 6 p.838 ~ p.844
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Purification and Biochemical Characteristics of Fibrinolytic Enzyme from Streptomyces corcohrussi JK-20
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Kim You-Jung
Choi Yung-Hyun
Park Jeong-Uck
Kim Min-Jeong
Lee Hye-Hyeon
Jin Se-Hun
Kang Byoung-Won
Jeong Yong-Kee
Seo Min-Jeong
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Abstract
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A fibrinolytic enzyme of Streptomyces corcohrussi from soil sediment was purified by chromatography using DEAE-Sephadex A-50 and Sephadex G-50. The analysis of SDS-polyacrylamide gel suggested that the purified enzyme is a homogeneous protein and the molecular mass is approximately 34 kDa. The purified enzyme showed activity of 0.8 U/ml in a plasminogen-rich fibrin plate, while its activity in a plasminogen-free fibrin plate was only 0.36 U/ml. These results suggested that the purified enzyme acts as a plasminogen activator. The fibrinolytic activity of the enzyme under the supplementation of protease inhibitors, ε-ACA, t-AMCHA and mercuric chloride in the enzyme reaction was less than 24%, indicating that it could be modulated by the plasmin and/or fibrinogen inhibitors involved in the fibrinogen-to-fibrin converting process. As time passed, Zn2+, a heavy metal ion, inhibited the activity to 34.1%. The optimum temperature of the purified enzyme was approximately 50℃ and over 92% of the enzyme activity was maintained between pH 5.0 and 8.0. Therefore, our results provide a potential fibrinolytic enzyme as a noble thrombolytic agent from S. corcohrussi.
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KEYWORD
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Fibrinolytic enzyme, plasmin inhibitor, plasminogen activator, Streptomyces corcohrussi
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