A functional proteomic analysis of secreted fibrinolytic enzymes from Bacillus subtilis 168 using a combined method of two-dimensional gel electrophoresis and zymography

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Title
A functional proteomic analysis of secreted fibrinolytic enzymes from Bacillus subtilis 168 using a combined method of two-dimensional gel electrophoresis and zymography
Author(s)
Sung Goo Park; Chang Won Ko; Sa Yeon Cho; Do Hee Lee; Seung Ho Kim; Byoung Chul Park
Bibliographic Citation
Proteomics, vol. 2, no. 2, pp. 206-211
Publication Year
2002
Abstract
Here we describe a proteomic approach to detect fibrinolytic enzymes from the culture supernatant of Bacillus subtilis 168. Following isoelectric focusing without dithiothreitol, two gels, one for sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and the other for zymography, were run in parallel. After silver staining of SDS-PAGE and activity staining of zymography gel, the two gels were superimposed to detect protein spots that coincided with clear zones on the zymography gel. We identified four protein spots and characterized them with matrix-assisted laser desorption/ ionization mass spectrometry. Database search revealed that four spots contained at least one of the extracellular serine proteases such as WprA and Vpr. This combined method of two-dimensional gel and zymography can be used as a powerful tool to detect proteases from various organisms.
Keyword
Fibrinolytic enzymesFunctional proteomicsMass spectrometryTwo-dimensional gel electrophoresisZymography
ISSN
1615-9853
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/1615-9861(200202)2:2<206::AID-PROT206>3.0.CO;2-5
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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