High performance liquid chromatography of biliprotein from Bangia atropurpurea ?Conchocelis?
Author(s) -
Hongg Chou,
Jiunn-Ming Jeng
Publication year - 1993
Publication title -
hydrobiologia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.843
H-Index - 141
eISSN - 1573-5117
pISSN - 0018-8158
DOI - 10.1007/bf00049072
Subject(s) - phycoerythrin , allophycocyanin , chromatography , chemistry , size exclusion chromatography , elution , phycocyanin , gel electrophoresis , polyacrylamide gel electrophoresis , isoelectric focusing , biology , biochemistry , cyanobacteria , flow cytometry , genetics , bacteria , enzyme
Gel-filtration-purified R-phycoerythrin and phycocyanin from the filamentous phase of Bangia atropurpurea were subjected to high performance anion exchange chromatographic separation. The purified R-phycoerythrin was a mixture of three charged-isomers that were well resolved in a Bio-Gel MA7P column by elution with a NaCl gradient in phosphate buffer. These were tentatively called phycoerythrin charged-isomers and were also separable from phycocyanin and allophycocyanin by the same system. Hence, it is suggested that the ion exchange chromatographic and the sample preparation methods presented in this report can be used to distinguish the various natures of biliproteins in red algae in addition to the polyacrylamide gel electrophoresis technique. Isomers of R-phycoerythrin have the same absorption and emission spectra and were studied for their subunit compositions by a PRP-3 reverse phase column chromatography. All three charged-isomers have the same α and β subunits in common but differ in their γ subunit.
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