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• W2070463524 abstract "The C-phycocyanin from the unicellular blue-green alga Phormidium luridum was isolated in high yield by an improved procedure as a crystalline protein, shown to be homogeneous by polyacrylamide gel electrophoresis. In common with C-phycocyanins from other blue-green algae (1–3), the protein from P. luridum was found to be an aggregate of two subunits, designated α and β, present in equivalent molar proportions. These subunits were separated preparatively by gel filtration in a solvent that contained sodium dodecylsulfate and β-mercaptoethanol. Chromatography on sulfonated polystyrene columns of tryptic hydrolyzates of the S-aminoethylated subunits afforded distinctly different elution patterns for each subunit. A combination of analytical gel filtration and amino acid analyses defined the molecular weights of the α and β subunits as 11,900 ± 100 and 18,500 ± 100, respectively. These weights include the contribution of a single phycocyanobilin chromophore in each subunit. Although generally similar in amino acid content, the two subunits display distinct differences in composition, notably in the absence of histidine from the β subunit. The results establish beyond reasonable doubt that the minimum molecular weight of ~30,000 previously (5) measured for this protein is actually the molecular weight of an aggregate of one of each of the subunits." @default.
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• W2070463524 date "1972-09-01" @default.
• W2070463524 modified "2023-09-23" @default.
• W2070463524 title "C-phycocyanin from Phormidium luridum. Isolation of subunits" @default.
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• W2070463524 doi "https://doi.org/10.1016/0003-9861(72)90207-x" @default.
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