8 Analytical Protocols in Phycobiliproteins Analysis
195
8.10 Conclusion
A recent increased interest in the use of PBPs for various industrial, biotechnological,
pharmaceutical, and clinical applications demands reliable experimental protocols
for their comprehensive analysis. The overview of traditional methods, as well as
the most recent experimental advances used for PBPs’ analysis given in this chapter,
may be useful for further scientific research of the role of PBPs in photosynthesis. In
addition, it may also serve as a literature guide for assembly of analytical protocols
for PBPs analysis prior to commercial and/or medical use.
Funding This work was supported by the Ministry of Education, Science and Technological
Development of the Republic of Serbia ( Contract number: 451-03-68/2020-14/200168). The project
leading to this application has received funding from the European Union’s Horizon 2020 research
and innovation program under grant agreement No 810752. The EC does not share responsibility
for the content of the article.
References
Adir, N., Vainer, R., & Lerner, N. (2002). Refined structure of c-phycocyanin from the cyanobacterium Synechococcus vulcanus at 1.6 angstrom: Insights into the role of solvent molecules in
thermal stability and co-factor structure. Biochimica et Biophysica Acta (BBA) - Bioenergetics,
1556, 168–174.
Aghtar, M., Strumpfer, J., Olbrich, C., Schulten, K., & Kleinekathofer, U. (2014). Different types
of vibrations interacting with electronic excitations in phycoerythrin 545 and Fenna-MatthewsOlson Antenna systems. The Journal of Physical Chemistry Letters, 5, 3131–3137.
Almog, R., Marsilio, F., & Berns, D. S. (1988). Interaction of C-phycocyanin with lipid monolayers
under nitrogen and in the presence of air. Archives of Biochemistry and Biophysics, 260, 28–36.
Angeleri, M., Muth-Pawlak, D., Aro, E. M., & Battchikova, N. (2016). Study of O-phosphorylation
sites in proteins involved in photosynthesis-related processes in synechocystis sp strain PCC
6803: Application of the SRM approach. Journal of Proteome Research, 15, 4638–4652.
Anwer, K., Sonani, R., Madamwar, D., Singh, P., Khan, F., Bisetty, K., et al. (2015). Role of
N-terminal residues on folding and stability of C-phycoerythrin: Simulation and urea-induced
denaturation studies. Journal of Biomolecular Structure & Dynamics, 33, 121–133.
Beer, S., & Eshel, A. (1985). Determining phycoerythrin and phycocyanin concentrations in aqueous
crude extracts of red algae. Australian Journal of Marine and Freshwater Research, 36, 785–793.
Bellissent-Funel, M. C. (2004). Internal motions in proteins: A combined neutron scattering and
molecular modelling approach. Pramana – Journal of Physics, 63, 91–97.
Benedetti, S., Benvenuti, F., Pagliarani, S., Francogli, S., Scoglio, S., & Canestrari, F. (2004).
Antioxidant properties of a novel phycocyanin extract from the blue-green alga Aphanizomenon
flos-aquae. Life Sciences, 75, 2353–2362.
Bennett, A., & Borogad, L. (1973). Complementary chromatic adaptation in a filamentous bluegreen
alga. Journal of Cell Biology, 58, 419–435.
Berkelman, T. R., & Lagarias, J. C. (1986). Visualization of bilin-linked peptides and proteins in
polyacrylamide gels. Analytical Biochemistry, 156, 194–201.
Berns, D. S., & MacColl, R. (1989). Phycocyanin in Physical-Chemical Studies. Chemical Reviews,
89, 807–825.
195
8.10 Conclusion
A recent increased interest in the use of PBPs for various industrial, biotechnological,
pharmaceutical, and clinical applications demands reliable experimental protocols
for their comprehensive analysis. The overview of traditional methods, as well as
the most recent experimental advances used for PBPs’ analysis given in this chapter,
may be useful for further scientific research of the role of PBPs in photosynthesis. In
addition, it may also serve as a literature guide for assembly of analytical protocols
for PBPs analysis prior to commercial and/or medical use.
Funding This work was supported by the Ministry of Education, Science and Technological
Development of the Republic of Serbia ( Contract number: 451-03-68/2020-14/200168). The project
leading to this application has received funding from the European Union’s Horizon 2020 research
and innovation program under grant agreement No 810752. The EC does not share responsibility
for the content of the article.
References
Adir, N., Vainer, R., & Lerner, N. (2002). Refined structure of c-phycocyanin from the cyanobacterium Synechococcus vulcanus at 1.6 angstrom: Insights into the role of solvent molecules in
thermal stability and co-factor structure. Biochimica et Biophysica Acta (BBA) - Bioenergetics,
1556, 168–174.
Aghtar, M., Strumpfer, J., Olbrich, C., Schulten, K., & Kleinekathofer, U. (2014). Different types
of vibrations interacting with electronic excitations in phycoerythrin 545 and Fenna-MatthewsOlson Antenna systems. The Journal of Physical Chemistry Letters, 5, 3131–3137.
Almog, R., Marsilio, F., & Berns, D. S. (1988). Interaction of C-phycocyanin with lipid monolayers
under nitrogen and in the presence of air. Archives of Biochemistry and Biophysics, 260, 28–36.
Angeleri, M., Muth-Pawlak, D., Aro, E. M., & Battchikova, N. (2016). Study of O-phosphorylation
sites in proteins involved in photosynthesis-related processes in synechocystis sp strain PCC
6803: Application of the SRM approach. Journal of Proteome Research, 15, 4638–4652.
Anwer, K., Sonani, R., Madamwar, D., Singh, P., Khan, F., Bisetty, K., et al. (2015). Role of
N-terminal residues on folding and stability of C-phycoerythrin: Simulation and urea-induced
denaturation studies. Journal of Biomolecular Structure & Dynamics, 33, 121–133.
Beer, S., & Eshel, A. (1985). Determining phycoerythrin and phycocyanin concentrations in aqueous
crude extracts of red algae. Australian Journal of Marine and Freshwater Research, 36, 785–793.
Bellissent-Funel, M. C. (2004). Internal motions in proteins: A combined neutron scattering and
molecular modelling approach. Pramana – Journal of Physics, 63, 91–97.
Benedetti, S., Benvenuti, F., Pagliarani, S., Francogli, S., Scoglio, S., & Canestrari, F. (2004).
Antioxidant properties of a novel phycocyanin extract from the blue-green alga Aphanizomenon
flos-aquae. Life Sciences, 75, 2353–2362.
Bennett, A., & Borogad, L. (1973). Complementary chromatic adaptation in a filamentous bluegreen
alga. Journal of Cell Biology, 58, 419–435.
Berkelman, T. R., & Lagarias, J. C. (1986). Visualization of bilin-linked peptides and proteins in
polyacrylamide gels. Analytical Biochemistry, 156, 194–201.
Berns, D. S., & MacColl, R. (1989). Phycocyanin in Physical-Chemical Studies. Chemical Reviews,
89, 807–825.