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Large scale preparation of pure phycobiliproteins
Photosynthesis Research, 1987This paper describes simple procedures for the purification of large amounts of phycocyanin and allophycocyanin from the cyanobacterium Microcystis aeruginosa. A homogeneous natural bloom of this organism provided hundreds of kilograms of cells. Large samples of cells were broken by freezing and thawing.
M P, Padgett, D W, Krogmann
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2008
Phycobilins are light harvesting pigments of cyanobacteria and red algae. In cyanobacteria, four phycobiliproteins are organized in phycobilisomes: phycocyanin (PC), allophycocyanin (APC), and often also phycoerythrocyanin (PEC) or phycoerythrin (PE).
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Phycobilins are light harvesting pigments of cyanobacteria and red algae. In cyanobacteria, four phycobiliproteins are organized in phycobilisomes: phycocyanin (PC), allophycocyanin (APC), and often also phycoerythrocyanin (PEC) or phycoerythrin (PE).
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Evolution of Phycobiliproteins
2017In genomic analysis, nucleotides may influence amino acid residue variability and functional codon usage of PC, PE, and APC that may take part in evolution. The large diversity of phycobiliproteins (PBPs) pigmentation is to facilitate through gene exchanges in lineages that maintain the diversity of micro-marine environment.
Vinod K. Kannaujiya +2 more
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Phycobiliproteins as Food Additives
2020The phycobiliproteins (FBPs) are antenna pigments composed of apoprotein covalently bound to phycobilin (tetrapyrrole chain chromophores). The main FBPs are phycoerythrin (PE), phycocyanin (PC), and allophycocyanin (APC) that absorb at 550, 620, and 650 nm, respectively, and are associated with phycobilisomes in cyanobacteria and rhodophytes.
null Alexandra Galetović C. +1 more
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Photostability studies of phycobiliprotein fluorescent labels
Analytical Biochemistry, 1987Photostability studies of four fluorescent phycobiliproteins were conducted to identify stable chromophores for biological labeling applications. Phycobiliprotein photodestruction was linear with the applied laser power and depended on the total number of photons absorbed per molecule.
J C, White, L, Stryer
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Stress Response of Phycobiliproteins
2017Phycobiliproteins (PBPs) are water-soluble, brilliantly colored pigmented protein complexes functioning as predominant accessory light-harvesting complexes to harvest the photonic energy of sunlight for photosynthesis. In the past few years, PBPs contribute a major role in the development of commercial colored food products, nutraceuticals, and ...
Vinod K. Kannaujiya +2 more
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Evaluation ofTolypothrix germplasm for phycobiliprotein content
Folia Microbiologica, 2003Twenty Tolypothrix strains, including 15 strains of T. tenuis, three strains of T. ceylonica and one strain each of T. nodosa and T. bouteillei, were evaluated for their phycobiliprotein content and composition. Significant differences among the Tolypothrix strains were found at both inter- and intra-specific levels in the production of ...
R, Prasanna +3 more
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