상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Detection of a unique fibrinolytic enzyme in Aeromonas sp. JH1

Authors 

Han-Young ChoM J SeoJ U ParkB W KangG Y KimW H JooY C LeeY S ChoY K Jeong

Publisher 

Microbiological Society of Korea

Issue Date 

2011

Citation 

Journal of Microbiology, vol. 49, no. 6, pp. 1018-1021

Keywords 

Aeromonas sp. JH1Amidolytic activityfibrinogen subunitsfibrinolytic enzymeN-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.

ISSN 

1225-8873

Link 

http://dx.doi.org/10.1007/s12275-011-1376-7

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)