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Team:USTC/Project/shell/result
From 2010.igem.org
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In the expression of protein, we use and unite the method mentioned in the previous papers. [see protocol] The bacterial was induced by 1 mM IPTG at 30 ℃ for 4 hours. The results was as follows.[the one without pduN was a negative control used to prove the function of pduN: in the growth process, the one without pduN tends to grow with more deposit implying its possible role in the vertex] | In the expression of protein, we use and unite the method mentioned in the previous papers. [see protocol] The bacterial was induced by 1 mM IPTG at 30 ℃ for 4 hours. The results was as follows.[the one without pduN was a negative control used to prove the function of pduN: in the growth process, the one without pduN tends to grow with more deposit implying its possible role in the vertex] | ||
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[[Image:Pdu_iptg.jpg| SDS-PAGE of pdu proteins]] | [[Image:Pdu_iptg.jpg| SDS-PAGE of pdu proteins]] | ||
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We use the ultracentrifuge to purify the proteins, with 48000 g speed, we get our targeted proteins in the pellet. | We use the ultracentrifuge to purify the proteins, with 48000 g speed, we get our targeted proteins in the pellet. | ||
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[[Image:Pdu_Sds-page.jpg| SDS-PAGE of pdu proteins]] | [[Image:Pdu_Sds-page.jpg| SDS-PAGE of pdu proteins]] | ||
Revision as of 03:33, 28 October 2010
In the expression of protein, we use and unite the method mentioned in the previous papers. [see protocol] The bacterial was induced by 1 mM IPTG at 30 ℃ for 4 hours. The results was as follows.[the one without pduN was a negative control used to prove the function of pduN: in the growth process, the one without pduN tends to grow with more deposit implying its possible role in the vertex]
We use the ultracentrifuge to purify the proteins, with 48000 g speed, we get our targeted proteins in the pellet.
