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Biological Applications of Diamond
Published in James C Sung, Jianping Lin, Diamond Nanotechnology, 2019
Using detonation ND, Bondar and coworkers14 successfully separated recombinant Ca2+-activated photoprotein apoobelin and recombinant luciferase from bacterial cells of Escherichia coli through physical absorption of proteins on ND. For traditional purification by chromatographic means, it usually takes several days. Figure 8.14 shows the procedures using ND. The cells were disrupted through ultrasound and the cell debris was removed by centrifugations. Then suspended detonation ND was added and then centrifuge to separate ND with protein absorbed on it. When treated by a selective block of SH group such as dithiothreitol, protein was desorbed from ND. The whole process took 30–40 min with a yield of 35–60%.
Fluorescent Proteins
Published in Guy Cox, Fundamentals of Fluorescence Imaging, 2019
The first step in what has often been termed as the “GFP revolution” in cell biology was made by Osamu Shimomura in 1961, when he discovered a green fluorescent protein accidentally in a bioluminescent jellyfish Aequorea victoria (avGFP) while studying aequorin, a chemoluminescent calcium-activated photoprotein [13]. Aequorin and GFP were found localized in the jellyfish light organs and blue fluorescent emissions by aequorin were shown to excite green GFP fluorescence by Förster resonance energy transfer between the two molecules [14]. Another GFP-type protein was found in a bioluminescent relative of corals, the sea pansy Renilla reniformis [15], and it likewise transforms blue light emitted by luciferase into green light. Since both proteins form components of a bioluminescent system, it was assumed that GFPs were restricted to bioluminescent organisms.
Improving the soluble expression of aequorin in Escherichia coli using the chaperone-based approach by co-expression with artemin
Published in Preparative Biochemistry and Biotechnology, 2018
Elaheh Khosrowabadi, Zeinab Takalloo, Reza H. Sajedi, Khosro Khajeh
Aequorin is a photoprotein originally isolated from the bioluminescent jellyfish Aequorea victoria.[20] This calcium-activated photoprotein is widely used for its unique advantages, such as detection within few seconds at the attomole level, high sensitivity and low background noise, high quantum yield, being active at physiological pH, and harmless application.[13–15] Additionally, aequorin has numerous applications in cell trafficking, biosensing, and immunoassays.[20] Despite the vast application of aequorin, this protein is susceptible to aggregation and proteolysis degradation[15] and a high level of the protein mostly accumulates in an insoluble form when it is over-expressed in bacterial cells. Therefore, in some previous studies, several approaches were used to improve its soluble expression.[21–23] In the present work, we have attempted to increase the yield of soluble, correctly folded aequorin produced in E. coli cells following its simultaneous expression with artemin using the single and multiple plasmid-based strategies. Therefore, artemin along with aequorin was co-expressed under the optimal expressing conditions to decrease the inclusion body formation of aequorin and increase its soluble content.