Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10844042 | Protein Expression and Purification | 2005 | 7 Pages |
Abstract
We have previously reported a proteomic approach to detect fibrinolytic enzymes from the secreted proteins of Bacillus subtilis 168 and identified two extracellular fibrinolytic enzymes of Bacillus, namely, Vpr and WprA. In this study, to confirm the fibrinolytic activity of Vpr, we cloned the vpr gene and expressed it in Escherichia coli, where it is predominantly localized to inclusion bodies. After affinity purification and desalting steps, the expressed Vpr is auto-processed to an active form. Interestingly, after the desalting step, several additional bands with fibrinolytic activity were detected in zymography gel along with a mature form (68Â kDa) of Vpr. MALDI-TOF analyses of these bands revealed that Vpr could exist in multiple forms.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Chang Won Kho, Sung Goo Park, Sayeon Cho, Do Hee Lee, Pyung Keun Myung, Byoung Chul Park,