Team:Macquarie Australia/Results
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- | <center><a name="2"><h3>Characterisation of Heme Oxygenase</h3></center><hr> | + | <center><a name="2"><h3>Characterisation of Heme Oxygenase</h3></center> |
+ | <p>The Heme Oxygenase produced was characterised with ALA and IPTG to determine if it was functional. | ||
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<center><a name="3"><h3>Bacteriophytochromes</h3></center> | <center><a name="3"><h3>Bacteriophytochromes</h3></center> | ||
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<center><a name="4"><h3>Bacteriophytochrome Characterisation</h3></center> | <center><a name="4"><h3>Bacteriophytochrome Characterisation</h3></center> |
Revision as of 04:23, 19 September 2012
Results and Characterisation
Results |
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Heme Oxygenase |
Bacteriophytochrome | Characterisation |
Heme Oxygenase |
Bacteriophytochrome |
Heme Oxygenase
We produced a Heme oxygenase that was codon optimize for E. coli. The Gibson assembly of the T7 promoter containing Heme Oxygenase was successful. The transformation was successful with numerous colonies grown using Chloramphenicol as the selecting agent. Six colonies were selected and then they were sequenced before digestion with EcoR1 and Spe1. The sequencing suggested that all of the colonies contained the plasmid with a Heme oxygenase identical to the original protein sequence. The gel containing the digested Heme Oxygenase bearing plasmid can be seen in Figure 1.
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Figure 1: The restriction digest showing the linearised plasmid backbone (Black Box) and the heme oxygenese gene (Green Box) |
Characterisation of Heme Oxygenase
The Heme Oxygenase produced was characterised with ALA and IPTG to determine if it was functional.