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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

Authors 

Sung Goo ParkChang Won KoSa Yeon ChoDo Hee LeeSeung Ho KimByoung Chul Park

Publisher 

Wiley-Blackwell

Issue Date 

2002

Citation 

Proteomics, vol. 2, no. 2, pp. 206-211

Keywords 

fibrinolytic enzymesfunctional proteomicsmass spectrometrytwo-dimensional gel electrophoresiszymographydodecyl sulfate sodiumplasminbacillus subtilisnonhumanpolyacrylamide gel electrophoresis

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.

ISSN 

1615-9853

Link 

http://dx.doi.org/10.1002/1615-9861(200202)2:2<206::AID-PROT206>3.0.CO;2-5

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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