Follow-On Lab Report

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The purpose of these series of experiment was successful as seen from the results. The recombinant form of the green fluorescent protein was successfully expressed and purified from E. coli. Though a high yield and purity were not obtained, the qualitative monitoring of the rGFP activity was consistent with the quantitative values obtained. Qualitatively, the elution fraction E2 fluoresced the most when placed under a hand-held UV lamp. Quantitatively, E2 also had the highest activity with 41900 RFUs when read by a fluorescent microplate reader. One way to increase the yield of rGFP would be to increase the IPTG induction time. This would increase the amount of rGFP that is expressed and consequently increase the amount of rGFP that is purified. There were other things during the experiment such as contaminant proteins that could also have affected the yield of rGFP obtained. …show more content…

GFP or rGFP has several unique characteristics which makes it a good research tool. rGFP is a small protein that needs no cofactor for fluorescence and detection of this protein is also easy and inexpensive. As a follow-on experiment, how GFP can be used as a tag for proteins can be explored. In this experiment, we expressed GFP in E. coli. As a follow-on experiment, we could express GFP in other organisms and use that as a tag to investigate gene expression. GFP would be expressed in three marine bacteria from a lac or npt-2 promoter (Stretton, Serina et al.). The bacterial strains would then be tagged with GFP which enables the visualization and the monitoring of gene expression in living cells (Stretton, Serina et

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