Detection of a unique fibrinolytic enzyme in Aeromonas sp. JH1.
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.
Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology, Yusung, Daejeon 305-600, Republic of Korea.
Han-Young
HY
Cho
Min Jeong
MJ
Seo
Jeong Uck
JU
Park
Byoung Won
BW
Kang
Gi-Young
GY
Kim
Woo Hong
WH
Joo
Young-Choon
YC
Lee
Young-Su
YS
Cho
Yong Kee
YK
Jeong
D000333:Aeromonas / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004795:Enzyme Stability; D005340:Fibrinogen / Q000378:metabolism*; D005343:Fibrinolytic Agents / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D009835:Oligochaeta / Q000382:microbiology; D013696:Temperature
D001426:Bacterial Proteins; D005343:Fibrinolytic Agents; D005340:Fibrinogen