Comparison of the biliproteins from two strains of the thermophilic cyanophyte Synechococcus lividus.
C-Phycocyanins from two thermophilic strains of Synechococcus lividus that grow within different temperature ranges have been shown to be unalike. The aggregation ability of these two C-phycocyanins in sedimentation-velocity experiments varied dramatically. Surprisingly, the aggregation properties of mesophilic C-phycocyanins were found to lie between those of the two thermophilic proteins. Under identical conditions at pH7.0, one thermophilic protein (Sy I) was composed of 17S and larger aggregates, whereas the other (Sy III) was an almost homogeneous 6S aggregate. Mesophilic C-phycocyanins have a mixture of 6S, 11S and less stable 17S aggregates under these conditions. Amino acid analysis, absorption spectra, immunochemistry and fluorescence polarization all indicated differences in the composition and properties of the thermophilic proteins, which suggest that they have different modes of adaptation to very high temperatures. Allophycocyanins from the two strains of S. lividus were also purified and studied, but unlike the C-phycocyanins no major differences were found between them. Allophycocyanin was homogeneous at pH6.0, with a sedimentation coefficient of 5.54S and mol.wt. 1.03x10(5), as determined by sedimentation-equilibrium measurements.
D000596:Amino Acids / Q000032:analysis; D001654:Bile Pigments / Q000032:analysis*; D002499:Centrifugation, Density Gradient; D000458:Cyanobacteria / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D010940:Plant Proteins / Q000032:analysis* / Q000276:immunology; D013050:Spectrometry, Fluorescence; D013696:Temperature
D000596:Amino Acids; D001654:Bile Pigments; D010940:Plant Proteins