ArticlePloS one2014
Isolation, purification and properties of an R-phycocyanin from the phycobilisomes of a marine red macroalga Polysiphonia urceolata.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Phycobilisomes were prepared from a marine red macroalga Polysiphonia urceolata (P. urceolata) by sucrose step-gradient ultracentrifugation. From the prepared phycobilisomes, an R-phycocyanin was isolated by gel filtration on Sephadex G-150 and then purified by ion exchange chromatography on DEAE-Sepharose Fast Flow and native polyacrylamide gel electrophoresis (PAGE) performed in neutral buffer systems. The purified R-phycocyanins showed not only a homogeneous trimer of 136 kDa in gel filtration and a single band in native PAGE, but also exhibited one band at about pH 5.7 in native isoelectric focusing (IEF). By a gradient SDS-PAGE the purified R-phycocyanin was determined to contain one a subunit of 17.5 kDa (α17.5) and two b subunits of 21.3 kDa and 22.6 kDa (β21.3 and β22.6). The analysis from denaturing isoelectric focusing and two-dimension PAGE demonstrated that α17.5, β21.3 and β22.6 had their pIs of 6.4, 5.3 and 5.4, respectively. Furthermore, mass spectroscopy analysis of β21.3 and β22.6 by MALDI-TOF mass spectrometry demonstrated the two b subunits had differences in peptide mass fingerprinting. These results revealed that the prepared R-phycocyanins were composed of one a and two b subunits. (α17:53 β21:32 β22:61) and (α17:53 β21:31 β22:62), which have a structural foundation to show their pIs too close for them to be definitely resolved by native IEF, are postulated to be the most possible trimeric forms of the R-phycocyanins prepared from the phycobilisomes of P. urceolata.
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