Abstract
The endophytic cyanobacterium, Anabaena azollae, isolated from laboratory cultures of Azolla caroliniana Willd., contains three spectroscopically distinct biliproteins. About 70% of the biliprotein is c-phycocyanin (λmax 610 nm) and 13% is allophycocyanin (λmax 647 nm, shoulder 620 nm). A third pigment corresponds to phycoerythrocyanin (λmax 570 nm, shoulder 590 nm). In very dilute solutions of allophycocyanin, at constant pH and buffer strength, the 647 nm maximum disappears and a single λmax occurs at 615–620 nm. The 647 nm absorption maximum reappears upon concentrating the dilute solution. Very dilute solutions of phycoerythrocyanin exhibit a broad peak between 570 and 590 nm. Absorption spectra of c-phycocyanin are not significantly altered upon dilution. Fluorescence emission maxima of phycoerythrocyanin, c-phycocyanin, and allophycocyanin occur at 630 nm, 643 nm and 660 nm respectively, using 540 nm excitation. Two subunits, of molecular weight 16,500 (α) and 20,600 (β), are seen in c-phycocyanin upon dissociation with SDS. Dissociation of allophycocyanin and phycoerythrocyanin with SDS yields one sizeclass of subunits, with a molecular weight of about 17,500 for allophycocyanin and 18,000 for phycoerythrocyanin.
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Tyagi, V.V.S., Mayne, B.C. & Peters, G.A. Purification and initial characterization of phycobiliproteins from the endophytic cyanobacterium of Azolla . Arch. Microbiol. 128, 41–44 (1980). https://doi.org/10.1007/BF00422303
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DOI: https://doi.org/10.1007/BF00422303