Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 Mar 4;15:59. doi: 10.1186/s12866-015-0387-7

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© Mitchell et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

PMC Copyright notice

VieB does not disrupt the GST-VieS-C/VieA-His ₆ interaction. GST-VieS-C (lane 5–10) or GST alone (lane 11–14) bound to glutathione beads were incubated with either, pre-mixed 5 μM VieA-His₆ and 25 μM VieB (VieB), 5 μM VieA-His₆ alone (VieA) or 5 μM VieA-His₆ and 25 μM BSA (BSA). Reactions were washed with 150 μl of wash buffer five times and protein was eluted off the beads with 150 μl of elution buffer containing reduced glutathione. Samples were taken from the input (I), wash (W) and elution (E) fractions for analysis on 10% SDS Page gel stained with Lumitein protein stain^TM. VieB, VieA and BSA inputs are indicated by lanes 2–4, respectively. Percentage of VieA-His₆ bound is the average of four replicates with standard deviation shown below; gel shown is a representative of the replicates. Statistical significance was determined by one-way ANOVA and Dunn’s Multiple Comparison. M = protein standard.