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Volumn 9, Issue 2, 2014, Pages 184-192

Thermal and pH Stability of the B-Phycoerythrin from the Red Algae Porphyridium cruentum

Author keywords

B PE; Phycobiliprotein; Phycoerythrin; Stability

Indexed keywords

ALGAE; CONVERGENCE OF NUMERICAL METHODS; PH EFFECTS;

EID: 84901036925     PISSN: 15571858     EISSN: 15571866     Source Type: Journal    
DOI: 10.1007/s11483-014-9331-x     Document Type: Article
Times cited : (51)

References (33)
  • 1
    • 79960839976 scopus 로고    scopus 로고
    • Algal chemodiversity and bioactivity: sources of natural variability and implications for commercial application
    • D. B. Stengel, S. Connan, Z. A. Popper, Algal chemodiversity and bioactivity: sources of natural variability and implications for commercial application. Biotechnol. Adv. 29, 483-501 (2011).
    • (2011) Biotechnol. Adv. , vol.29 , pp. 483-501
    • Stengel, D.B.1    Connan, S.2    Popper, Z.A.3
  • 2
    • 79958255848 scopus 로고    scopus 로고
    • Microalgae as sources of high added-value compounds-a brief review of recent work
    • A. C. Guedes, H. M. Amaro, F. X. Malcata, Microalgae as sources of high added-value compounds-a brief review of recent work. Biotechnol Progr 27, 597-613 (2011).
    • (2011) Biotechnol Progr , vol.27 , pp. 597-613
    • Guedes, A.C.1    Amaro, H.M.2    Malcata, F.X.3
  • 3
    • 41049106722 scopus 로고    scopus 로고
    • Phycobiliproteins as a commodity: trends in applied research, patents and commercialization
    • S. Sekar, M. Chandramohan, Phycobiliproteins as a commodity: trends in applied research, patents and commercialization. J. Appl. Phycol. 20, 113-136 (2008).
    • (2008) J. Appl. Phycol. , vol.20 , pp. 113-136
    • Sekar, S.1    Chandramohan, M.2
  • 6
    • 0024202010 scopus 로고
    • Phycobiliproteins
    • A. N. Glazer, Phycobiliproteins. Methods Enzymol. 167, 291-303 (1988).
    • (1988) Methods Enzymol. , vol.167 , pp. 291-303
    • Glazer, A.N.1
  • 7
    • 0000620421 scopus 로고
    • J. R. Harris and R. W. Horne (Eds.), London: Academic Press
    • E. Mörschel, E. Rhiel, in Phycobilisomes and Thylakoids, ed. by J. R. Harris, R. W. Horne (Academic Press, London, 1987), p. 210.
    • (1987) Phycobilisomes and Thylakoids , pp. 210
    • Mörschel, E.1    Rhiel, E.2
  • 8
    • 0029910197 scopus 로고    scopus 로고
    • Cryptomonad biliproteins: bilin types and locations
    • G. J. Wedemayer, D. G. Kidd, A. N. Glazer, Cryptomonad biliproteins: bilin types and locations. Photosynth. Res. 48, 163-170 (1996).
    • (1996) Photosynth. Res. , vol.48 , pp. 163-170
    • Wedemayer, G.J.1    Kidd, D.G.2    Glazer, A.N.3
  • 9
    • 0006911366 scopus 로고    scopus 로고
    • Natural pigments from red microalgae for food and cosmetics
    • In: Charalambous G, editor Amsterdam: Elsevier Science Publishers BV; 1993
    • A. Yaron and S. (M) Arad, Natural pigments from red microalgae for food and cosmetics. In: Charalambous G, editor. Food flavors, ingredients and composition. Amsterdam: Elsevier Science Publishers BV; 1993.
    • Food flavors, ingredients and composition
    • Yaron, A.1    Arad, S.M.2
  • 10
    • 84885180176 scopus 로고    scopus 로고
    • Health applications of bioactive compounds from marine microalgae
    • M. F. de Jesus Raposo, R. M. de Morais, A. M. de Morais, Health applications of bioactive compounds from marine microalgae. Life Sci. 93, 479-486 (2013).
    • (2013) Life Sci. , vol.93 , pp. 479-486
    • de Jesus Raposo, M.F.1    de Morais, R.M.2    de Morais, A.M.3
  • 13
    • 84878837218 scopus 로고    scopus 로고
    • Antitumor function and mechanism of phycoerythrin from Porphyra haitanensis
    • Q. Pan, M. Chen, J. Li, Y. Wu, C. Zhen, B. Liang, Antitumor function and mechanism of phycoerythrin from Porphyra haitanensis. Biol Res. 46, 87-95 (2013).
    • (2013) Biol Res. , vol.46 , pp. 87-95
    • Pan, Q.1    Chen, M.2    Li, J.3    Wu, Y.4    Zhen, C.5    Liang, B.6
  • 14
    • 0017597753 scopus 로고
    • Subunit structure and chromophore composition of rhodophytan phycoerythrins. B-phycoerythrin and b-phycoerythrin
    • A. N. Glazer, C. S. Hixson, Subunit structure and chromophore composition of rhodophytan phycoerythrins. B-phycoerythrin and b-phycoerythrin. J. Biol. Chem. 252, 32-42 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 32-42
    • Glazer, A.N.1    Hixson, C.S.2
  • 15
    • 0024989528 scopus 로고
    • Separation of phycobiliprotein subunits by reverse-phase high-pressure liquid chromatography
    • R. W. Swanson, A. N. Glazer, Separation of phycobiliprotein subunits by reverse-phase high-pressure liquid chromatography. Anal. Biochem. 188, 295-299 (1990).
    • (1990) Anal. Biochem. , vol.188 , pp. 295-299
    • Swanson, R.W.1    Glazer, A.N.2
  • 16
    • 0027509158 scopus 로고
    • Rod structure of phycoerythrin II-containing phycobilisome II, Complete sequence and bilin attachment site of a phycoerythrin γ-subunit
    • S. M. Wilbanks, A. N. Glazer, Rod structure of phycoerythrin II-containing phycobilisome II, Complete sequence and bilin attachment site of a phycoerythrin γ-subunit. J. Biol. Chem. 268, 1236-1241 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 1236-1241
    • Wilbanks, S.M.1    Glazer, A.N.2
  • 18
    • 0021346794 scopus 로고
    • Bilin attachment sites in the α- and β-subunits of B-phycoerythrin. Amino acid sequence studies
    • D. J. Lundell, A. N. Glazer, R. J. de Lange, D. M. Brown, Bilin attachment sites in the α- and β-subunits of B-phycoerythrin. Amino acid sequence studies. J. Biol. Chem. 259, 5472-5480 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 5472-5480
    • Lundell, D.J.1    Glazer, A.N.2    de Lange, R.J.3    Brown, D.M.4
  • 20
    • 0035844078 scopus 로고    scopus 로고
    • Chromatographic purification and characterization of B-phycoerythrin from Porphyridium cruentum. Semipreparative high-performance liquid chromatographic separation and characterization of its subunits
    • R. Bermejo, E. M. Talavera, J. M. Álvarez Pez, Chromatographic purification and characterization of B-phycoerythrin from Porphyridium cruentum. Semipreparative high-performance liquid chromatographic separation and characterization of its subunits. J. Chrom. A. 917, 135-145 (2001).
    • (2001) J. Chrom. A. , vol.917 , pp. 135-145
    • Bermejo, R.1    Talavera, E.M.2    Álvarez Pez, J.M.3
  • 21
    • 0027373718 scopus 로고
    • Refined crystal structure of phycoerythrin from Porphyridium cruentum at 0.23-nm resolution and localization of the gamma subunit
    • R. Ficner, R. Huber, Refined crystal structure of phycoerythrin from Porphyridium cruentum at 0. 23-nm resolution and localization of the gamma subunit. Eur. J. Biochem. 218, 103-106 (1993).
    • (1993) Eur. J. Biochem. , vol.218 , pp. 103-106
    • Ficner, R.1    Huber, R.2
  • 24
    • 77958183202 scopus 로고    scopus 로고
    • Effect of preservatives for food grade C-Phycoerythrin, isolated from marine cyanobacteria Pseudanabaena sp
    • S. K. Mishra, A. Shrivastav, I. Pancha, D. Jain, S. Mishra, Effect of preservatives for food grade C-Phycoerythrin, isolated from marine cyanobacteria Pseudanabaena sp. Int. J. Biol. Macromol. 47, 597-602 (2010).
    • (2010) Int. J. Biol. Macromol. , vol.47 , pp. 597-602
    • Mishra, S.K.1    Shrivastav, A.2    Pancha, I.3    Jain, D.4    Mishra, S.5
  • 25
    • 84900988139 scopus 로고    scopus 로고
    • Procedimiento de purificación de biomoléculas que utiliza cromatografía de adsorción en lecho expandido
    • 2383866
    • M. J. Ibañez-Gonzalez, T. Mazzuca-Sobczuk, E. Molina-Grima, Procedimiento de purificación de biomoléculas que utiliza cromatografía de adsorción en lecho expandido. Patent ES 2383866, B1 (2013).
    • (2013) Patent ES
    • Ibañez-Gonzalez, M.J.1    Mazzuca-Sobczuk, T.2    Molina-Grima, E.3
  • 26
    • 0037972267 scopus 로고    scopus 로고
    • The inactivating factor of glutamine synthetase, IF7, is a "natively unfolded" protein
    • M. I. Muro-Pastor, F. N. Barrera, J. C. Reyes, F. J. Florencio, J. L. Neira, The inactivating factor of glutamine synthetase, IF7, is a "natively unfolded" protein. Protein Sci. 12, 1443-1454 (2003).
    • (2003) Protein Sci. , vol.12 , pp. 1443-1454
    • Muro-Pastor, M.I.1    Barrera, F.N.2    Reyes, J.C.3    Florencio, F.J.4    Neira, J.L.5
  • 28
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network
    • M. A. Andrade, P. Chacón, J. J. Merelo, F. Morán, Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network. Prot. Eng. 6, 383-390 (1993).
    • (1993) Prot. Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 29
    • 0033764779 scopus 로고    scopus 로고
    • pH affects the thermal inactivation parameters of R-phycoerythrin from Porphyra yezoensis
    • A. Orta-Ramirez, J. E. Merrill, D. M. Smith, pH affects the thermal inactivation parameters of R-phycoerythrin from Porphyra yezoensis. J. Food Sci. 65, 1046-1050 (2000).
    • (2000) J. Food Sci. , vol.65 , pp. 1046-1050
    • Orta-Ramirez, A.1    Merrill, J.E.2    Smith, D.M.3
  • 30
    • 0030579813 scopus 로고    scopus 로고
    • Comparative thermodynamic elucidation of the structural stability of thermophilic proteins
    • L. G. Roth, D. S. Berns, C. H. Chen, Comparative thermodynamic elucidation of the structural stability of thermophilic proteins. Biophys. Chem. 60, 89-97 (1996).
    • (1996) Biophys. Chem. , vol.60 , pp. 89-97
    • Roth, L.G.1    Berns, D.S.2    Chen, C.H.3
  • 31
    • 0017726227 scopus 로고
    • The quaternary structure of a unique phycobiliprotein: B-phycoerythrin from Porphyridium cruentum
    • C. Abad-Zapatero, J. L. Fox, M. L. Hackert, The quaternary structure of a unique phycobiliprotein: B-phycoerythrin from Porphyridium cruentum. Biochem. Biophys. Res. Commun. 78, 266-272 (1977).
    • (1977) Biochem. Biophys. Res. Commun. , vol.78 , pp. 266-272
    • Abad-Zapatero, C.1    Fox, J.L.2    Hackert, M.L.3
  • 32
    • 0016861704 scopus 로고
    • Characterization of R-phycocyanin. Chromophore content of R-phycocyanin and C-phycoerythrin
    • A. N. Glazer, C. S. Hixson, Characterization of R-phycocyanin. Chromophore content of R-phycocyanin and C-phycoerythrin. J. Biol. Chem. 250, 5487-5495 (1975).
    • (1975) J. Biol. Chem. , vol.250 , pp. 5487-5495
    • Glazer, A.N.1    Hixson, C.S.2
  • 33
    • 67649405075 scopus 로고    scopus 로고
    • Protein ionizable groups: pK values and their contribution to protein stability and solubility
    • C. N. Pace, G. R. Grimsley, J. M. Scholtz, Protein ionizable groups: pK values and their contribution to protein stability and solubility. J. Biol. Chem. 284, 13285-13289 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 13285-13289
    • Pace, C.N.1    Grimsley, G.R.2    Scholtz, J.M.3


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