상세 정보

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

Title 

Confirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis

Authors 

Chang Won KhoSung Goo ParkS ChoDo Hee LeeP K MyungByoung Chul Park

Publisher 

Elsevier

Issue Date 

2005

Citation 

Protein Expression & Purification, vol. 39, no. 1, pp. 1-7

Keywords 

fibrinolytic enzymesmass spectrometryserine proteaseVprzymographybacterial proteinserine proteinaseureaVpr protein, bacillus subtilisbacillus subtilis

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 (68 kDa) of Vpr. MALDI-TOF analyses of these bands revealed that Vpr could exist in multiple forms.

ISSN 

1046-5928

Link 

http://dx.doi.org/10.1016/j.pep.2004.08.008

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)