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
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- 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
- Nack-Shick Choi; Dong-Min Jeong; Chan Sun Park; Keug Hyun Ahn; Joong Su Kim; Jae Jun Song; Seung Ho Kim; Byung Dae Yoon; Min-Soo Kim
- Bibliographic Citation
- Biotechnology and Bioprocess Engineering, vol. 15, no. 3, pp. 446-452
- Publication Year
- 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.
- Bacillus subtilis; Mass spectrometry; UUG start codon; Vpr; Zymography
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- Jeonbuk Branch Institute > Immunoregulatory materials Research Center > 1. Journal Articles
Jeonbuk Branch Institute > Functional Biomaterial Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
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