Differentiation between Phycobiliprotein and Colorless Linker Polypeptides by Fluorescence in the Presence of ZnSO(4) |
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Authors: | Raps S |
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Institution: | Department of Biological Sciences, Hunter College, CUNY, New York, New York 10021. |
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Abstract: | Microcystis aeruginosa, a unicellular cyanobacterium, contains small phycobilisomes consisting of C-phycocyanin, allophycocyanin, and linker polypeptides. SDS-polyacrylamide gels of the phycobilisomes were examined for fluorescent bands before and after spraying with a solution of ZnSO4, followed by Coomassie brilliant blue staining for protein. This procedure provides a rapid and sensitive method for detecting small amounts of phycobilin-containing polypeptides and distinguishing them from other tetrapyrrole-containing polypeptides and from `colorless' ones. Three polypeptide bands, in addition to the α and β phycobiliprotein subunits, have been detected under these conditions. An 85 kilodalton polypeptide was identified as a phycobiliprotein due to its enhanced fluorescence in the presence of ZnSO4. The other polypeptides do not contain chromophores and are colorless. They are approximately 34.5 and 30 kilodaltons in size. |
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