Abstract
There are two spectral types of R-phycoerythrin (RPE) in red algae. One is the triple peak type RPE with absorption maxima at 498,540 and 565 nm. The other is the double peak type RPE with absorption maxima at 498 and 565 nm, and an absorption shoulder at 540 nm. The former is present only in higher classes of the more advanced Florideophyceae, the latter occurs chiefly in the more primitive Bangiophyceae. When these two types of RPE are treated with buffer solutions with a broad pH range from 2.0 to 11.0, their absorption and fluorescence spectra remain unchanged within the range adjacent to neutral pH. At pH values higher than 9.6, the absorption and fluorescence spectra of triple peak type RPE still remain stable, but the absorption spectra of double peak type RPE produce gradually a protrusion similar to an absorption peak at about 540 nm. This phennomenon shows that there are certain differences in structure between these two types of RPE. Both types of RPE are naturally occurring products showing systematic developmental meaning in red algae.
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References
Bennett, A. and L. Bogored, 1971. Properties of subunits aggregated of blue-green algae biliproteins.Biochem. 10:3625–3635.
Eriksson-quensel, I.B., 1938.Biochem. J.,32:585–589.
Frackowiak, D., 1979. Spectral properties of phycoerythrin.Photosynthetica 13 (1):21–28.
Gantt, E., Lipschultz, C.A., Zilinakas, B., 1976. Further evidence for a phycibilisome model from selective dissociation, fluorescence emission, immunoprecipitation, and electron microscopy.Biochem. Biophys. Acta 430:375–388.
Glazer, A.N., Fang, S. and D.W. Brown, 1973. Spectroscopic properties of C-phycoctanin and of its α and β subunits.J. Biol. Chem. 430:375–388.
Glazer, A.N., 1981. Photosynthetic Accessory Protein with Biliprosthetic Groups. in the Biochemistry of Plants, Vol. 8, edited by Hatch, N.D. and N.K. Boardman. Academic Press, New York, pp. 51–92.
Hattori, J., Crespi, H.L. and J.J. Katz, 1965. Association and dissociation of phycocyanin and the effect of deuterium substitution on the processes.Biochem. 4:1225–1236.
Haxo, H.T. and C. O’hEocha, 1960. Chromoproteins of Algae. in Encyclopedia of Plant Physiology Vol. 5, edited by Ruland, W., Springer-Verlag, Berlin, pp. 497–510.
Hirose, H. and S. Kumano, 1966. Photoreactive pigments of algae and phylogeny, in Advance of phycology in Japan. edited by Tokara, Veb Gustav Fisher verlag jana, pp. 52–56.
Krasnovskii, A.A., V.B. Evstigneev, G.P. Brin, et al., 1952. Isolation of phycoerythrin from red algae and its spectral and photochemical properties.Dok. Akad. Nauk. SSSR,82(6):974–950.
Murakami, A., Mimuro, M. and K. Ohki et al., 1981. Absorption spectrum of allophycocyanin isolated from Anabaena cylidrica: variation of the absorption spectrum induced by change of physicochemical environmentJ. Biochem.,89:79–86.
O’hEocha, C., 1962. Phycobilin, in Physiology and Biochemistry of Algae. edited by Lewin, R.A., Acad. Press, New York and London, pp. 421–435.
Vaughan, M.H.,jr. 1964. Ph.D. Thesis, Massachusetts institute of technology, Cambridge.
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Contribution No. 1333 from the Institute of Oceanology, Academic Sinica.
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Zhongzheng, P., Baicheng, Z., Chengkui, Z. et al. The effect of pH on both spectral types of R-phycoerythrin. Chin. J. Ocean. Limnol. 5, 73–79 (1987). https://doi.org/10.1007/BF02848525
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DOI: https://doi.org/10.1007/BF02848525