Difference between revisions of "Team:Lethbridge HS/Results"
MinaAkbary (Talk | contribs) |
|||
| Line 88: | Line 88: | ||
<p style="font-size: 3vw; font-family: 'Open Sans'">PROTEIN PURIFICATION</p> | <p style="font-size: 3vw; font-family: 'Open Sans'">PROTEIN PURIFICATION</p> | ||
| − | <p style="font-size: | + | <p style="font-size: 18px; font-family: 'Open Sans'"> |
One of the major aspects of our system utilizes metal binding proteins, so it was imperative that we purify the protein in order to move forward and complete our Copper Binding Assay. Our team successfully purified the Cut A protein through Nickel Affinity Chromatography (link) and Size Exclusion Chromatography (link). | One of the major aspects of our system utilizes metal binding proteins, so it was imperative that we purify the protein in order to move forward and complete our Copper Binding Assay. Our team successfully purified the Cut A protein through Nickel Affinity Chromatography (link) and Size Exclusion Chromatography (link). | ||
Revision as of 06:09, 17 October 2018
PROTEIN PURIFICATION
One of the major aspects of our system utilizes metal binding proteins, so it was imperative that we purify the protein in order to move forward and complete our Copper Binding Assay. Our team successfully purified the Cut A protein through Nickel Affinity Chromatography (link) and Size Exclusion Chromatography (link). The CutA protein was expressed in BL21 E.coli cells, and those cells were lysed then centrifuged to separate the supernatant and cell pellet. The lysate was then introduced to a Nickel Sepharose affinity column to isolate the CutA protein as it was bound to the Nickel Sepharose by its histidine tag. Then after washing to remove the unwanted proteins and cell debris, the CutA protein was eluted from the Nickel Sepharose.