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KMID : 0880220110490061018
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Journal of Microbiology
2011 Volume.49 No. 6 p.1018 ~ p.1021
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Detection of a unique fibrinolytic enzyme in Aeromonas sp. JH1
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Cho Han-Young
Seo Min-Jeong
Park Jeong-Uck
Kang Byoung-Won
Kim Gi-Young
Joo Woo-Hong
Lee Young-Choon
Cho Young-Su
Jeong Yong-Kee
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Abstract
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A fibrinolytic enzyme was found in a Gram-negative bacterium, Aeromonas sp. JH1. SDS-PAGE and fibrinzymography showed that it was a 36 kDa, monomeric protein. Of note, the enzyme was highly specific for fibrinogen molecules and the hydrolysis rate of fibrinogen subunits was highest for α, β, and γ chains in that order. The first 15 amino acids of N-terminal sequence were X-D-A-T-G-P-G-G-N-V-X-T-G-K-Y, which was distinguishable from other fibrinolytic enzymes. The optimum pH and temperature of the enzyme were approximately 8.0 and 40°C, respectively. Therefore, these results provide a fibrinolytic enzyme with potent thrombolytic activity from the Aeromonas genus.
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KEYWORD
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Amidolytic activity, Aeromonas sp. JH1, fibrinogen subunits, fibrinolytic enzyme, N-terminal amino acid sequence
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