Detection of a unique fibrinolytic enzyme in Aeromonas sp. JH1

Cited 2 time in scopus
Metadata Downloads
Title
Detection of a unique fibrinolytic enzyme in Aeromonas sp. JH1
Author(s)
Han Young Cho; M J Seo; J U Park; B W Kang; G Y Kim; W H Joo; Y C Lee; Y S Cho; Y K Jeong
Bibliographic Citation
Journal of Microbiology, vol. 49, no. 6, pp. 1018-1021
Publication Year
2011
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.
Keyword
Aeromonas sp. JH1Amidolytic activityfibrinogen subunitsfibrinolytic enzymeN-terminal amino acid sequence
ISSN
1225-8873
Publisher
Microbiological Society Korea
DOI
http://dx.doi.org/10.1007/s12275-011-1376-7
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.