B-Phycoerythrin from Rhodella violacea: characterization of two isoproteins.

Archives of Microbiology
K P Koller, W Wehrmeyer

Abstract

Two isoproteins of the "native" B-phycoerythrin of the red alga, Rhodella violacea, were purified from crude extracts by preparative polyacrylamide gel electrophoresis and subsequently characterized. The slower moving pigment in gel electrophoresis was designated B-PE I, the faster as B-PE II. Both were found to occur in about equal amounts. B-PE I has a molecular weight of about 280000 and an IEP at 4.39, B-PE II a molecular weight of nearly 265000 and an IEP at 4.23. B-PE I and II are characterized by absorption maxima at 568 and 542 nm and a shoulder at 500 nm in the visible part of the absorption spectra. Their absorption coefficients at 542 nm differ with values of 5.54 and 5.63, respectively. The fluorescence emission spectra show a single maximum at 575 for B-PE I and at 578 nm for B-PE II. Both spectra have a shoulder at 630 nm. The fluorescence yield of B-PE II is lower by 25%. In calibrated SDS gel electrophoresis of the purified pigments B-PE I and II show two subunits of molecular weights of 18900 and 29200 and 18500 and 29900, respectively. Quantitative amino acid analyses indicated, that the isoproteins are very similar. B-PE II, however, has a significantly higher content of acidic amino acids and a lower percent...Continue Reading

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Citations

May 13, 1977·Archives of Microbiology·E Mörschel, W Wehrmeyer
Jul 20, 2004·Skin Pharmacology and Physiology·Q C HeA Tavakkol
Nov 3, 2001·Journal of Biotechnology·R Bermejo RománE Molina Grima
May 28, 2003·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Ruperto BermejoJosé M Alvarez-Pez
Nov 1, 1976·Archives of Biochemistry and Biophysics·R MacCollO Gibbons
Mar 30, 2006·Protein Expression and Purification·Jian-Feng NiuCheng-Kui Tseng

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