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KMID : 0880220100480060836
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Journal of Microbiology
2010 Volume.48 No. 6 p.836 ~ p.841
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Purification and biochemical characterization of a 17 kDa fibrinolytic enzyme from Schizophyllum commune
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Park In-Suk
Park Jeong-Uck
Seo Min-Jeong
Kim Min-Jeong
Lee Hye-Hyeon
Kim Sung-Ryeal
Jeong Yong-Kee
Kang Byoung-Won
Choi Yung-Hyun
Joo Woo-Hong
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Abstract
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A fibrinolytic enzyme of the mushroom, Schizophyllum commune was purified with chromatographic methods, including a DEAE-Sephadex A-50 ion-exchange column and gel filtrations with Sephadex G-75 and Sephadex G-50 columns. The analysis of fibrin-zymography and SDS-PAGE showed that the enzyme was a monomeric subunit that was estimated to be approximately 17 kDa in size. The fibrinolytic activity of the enzyme in plasminogen-rich and plasminogen-free fibrin plates was 1.25 and 0.44 U/ml, respectively. The N-terminal amino acid sequence of the purified enzyme was identified as HYNIXNSWSSFID, which was highly distinguished from known fibrinolytic enzymes. The relative activity of the purified enzyme with an addition of 5 mM EDTA, Phosphoramidon, and Bestatin was about 76, 64, and 52%, respectively, indicating that it is a metalloprotease. The optimum temperature for the purified enzyme was approximately 45°C, and over 87% of the enzymatic activity was maintained as a stable state in a pH range from 4.0 to 6.0. Therefore, our results suggest that the potential thrombolytic agent from S. commune is a unique type of fibrinolytic enzyme.
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KEYWORD
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fibrinolytic enzyme, fibrin-zymography, N-terminal amino acid sequence, mushroom, S. commune
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