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Title 

Expression and identification of a minor extracellular fibrinolytic enzyme (Vpr) from Bacillus subtilis KCTC 3014

 

Bacillus subtilis KCTC3014 유래 세포 외 분비형 혈전용해 부효소의 동정 및 발현

Authors 

Nack-Shick ChoiDong-Min JeongChan Sun ParkKeug Hyun AhnJoong Su KimJae Jun SongSeung Ho KimByung Dae YoonMin-Soo Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

2010

Citation 

Biotechnology and Bioprocess Engineering, vol. 15, no. 3, pp. 446-452

Keywords 

Bacillus subtilisMass spectrometryUUG start codonVprZymography

Abstract 

Previously, three extracellular proteases, Vpr, PepT, and subtilisin were identified from Bacillus subtilis KCTC 3014. To confirm the activity of Vpr, two recombinant Vpr proteins, full Vpr with TTG (pGST-fTTG-Vpr) and full Vpr with ATG (pGST-fATG-Vpr) as an initiation codon were expressed using a pGEX-2T vector encoding glutathione S-transferase (GST) in Escherichia coli. Vpr was produced in two forms, occurring as four spots on a 2- DE gel, 68 and 75 kDa proteins with similar pI values (4.0 ? 4.5). Activity was detected in a fibrin zymography at the expected molecular size of 68 kDa (mature form) processed from full Vpr. However, the recombinant 75 kDa of GST-fVpr did not exhibit activity. Replacement of the TTG codon with ATG led to 1.9-fold increased enzyme activity in 68 kDa. Interestingly, the expression of GSTVpr resulted in the proteolytic degradation of the protein and no GST fusion Vpr protein was detected.

ISSN 

1226-8372

Link 

http://dx.doi.org/10.1007/s12257-009-0191-z

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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