| Title |
NOTE] Detection of a Unique Fibrinolytic Enzyme in Aeromonas sp. JH1 |
| Author |
Han-Young Cho1, Min Jeong Seo2,3,4, Jeong Uck Park4, Byoung Won Kang4, Gi-Young Kim5, Woo Hong Joo6, Young-Choon Lee2,3,4, and Yong Kee Jeong2,3,4* |
| Address |
1Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology, Yusung, Daejeon 305-600, Republic of Korea, 2Department of Biotechnology, Dong-A University, Busan 604-714, Republic of Korea, 3Department of Medical Bioscience, Dong-A University, Busan 604-714, Republic of Korea, 4Medi-Farm Industrialization Research Center, Dong-A University, Busan 604-714, Republic of Korea, 5Laboratory of Immunobiology, Department of Marine Life Sciences, Jeju National University, Jeju 690-756, Republic of Korea, 6Department of Biology, Changwon National University, Kyungnam 641-713, Republic of Korea |
| Bibliography |
Journal of Microbiology, 49(6),1018-1021, 2011,
|
| DOI |
|
| Key Words |
Amidolytic activity, Aeromonas sp. JH1, fibrinogen subunits, fibrinolytic enzyme, N-terminal amino acid sequence |
| Abstract |
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. |
