|
KMID : 0613820100200020183
|
|
Journal of Life Science
2010 Volume.20 No. 2 p.183 ~ p.189
|
|
|
Purification and Biochemical Characteristics of a 45 kDa Fibrinolytic Enzyme from a Halophile
|
|
Kim Do-Hyoung
Park Jeong-Uck
Seo Min-Jeong
Kim Min-Jung
Lee Hye-Hyeon
Choi Yung-Hyun
Joo Woo-Hong
Jeong Yong-Kee
|
|
|
Abstract
|
|
|
|
A fibrinolytic enzyme producing Bacillus sp. J-19 was isolated from the popular Korean seasoning, pickled anchovy. The fibrinolytic enzyme was purified to homogeneity by chromatographic methods including ethanol precipitation and gel-filtration using Sephadex G-50. Compared to the crude enzyme extract, the specific activity of the enzyme increased 1021-fold with a recovery of 23%. The purified enzyme was estimated to be approximately 45 kDa by SDS-PAGE. Especially, the amidolytic activity in the presence of the synthetic substrate for serine protease (H-D-Ile-Pro-Arg-pNA, S-2288) represented approximately 17 U/㎎. In addition, more than the 60% activity of the 45 kDa fibrinolytic activity was maintained in the presence of up to 30% (w/v) sodium chloride. These findings could provide a unique fibrinolytic enzyme, leading to a potential thrombolytic agent.
|
|
|
KEYWORD
|
|
|
Amidolytic activity, Bacillus sp., fibrinolytic enzyme, halophile, serine protease
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|