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Showing 1 to 12 of 12 for “"Phycobiliproteins"”.

  1. Identification and characterization of enzymes involved in the biosynthesis of different phycobiliproteins in cyanobacteria

    … used to recreate the biosynthetic pathway for phycobiliproteins from the cyanobacterium Synechococcus sp. PCC 7002 in <em><em>E. coli</em></em>. This system efficiently produced chromophorylated allophycocyanin (ApcA/ApcB), -phycocyanin, and -phycocyanin. This system was used to demonstrate …

    uno Repository record for Identification and characterization of enzymes involved in the biosynthesis of different phycobiliproteins in cyanobacteria (opens in a new tab)

  2. CE-LIF ANALYSIS OF INTACT MARINE MICROBES ALONG WITH THEIR CONSTITUENT PHYCOBILIPROTEINS AND PHYCOBILIN PIGMENTS

    … and quantitation of their natively fluorescent phycobiliproteins, and 2) their electrophoretic profiles as intact organisms. CE-LIF results were compared to those obtained by way of a newly developed, high efficiency separation method known as polymer enhanced capillary transient …

    wfu Repository record for CE-LIF ANALYSIS OF INTACT MARINE MICROBES ALONG WITH THEIR CONSTITUENT PHYCOBILIPROTEINS AND PHYCOBILIN PIGMENTS (opens in a new tab)

  3. Identification and Characterization of Enzymes Involved in Post-translational Modifications of Phycobiliproteins in the Cyanobacterium Synechocystis sp. PCC 6803

    … for posttranslational modifications of phycobiliproteins (PBP) in the cyanobacterium Synechocystis sp. PCC 6803. Asparagine 72 is methylated to produce gamma-N-methylasparagine on beta subunits of PBP in vivo. A candidate for this methyl transferase is CpcM (sll0487). Methylase assays …

    uno Repository record for Identification and Characterization of Enzymes Involved in Post-translational Modifications of Phycobiliproteins in the Cyanobacterium Synechocystis sp. PCC 6803 (opens in a new tab)

  4. Identification and Characterization of a New Class of Bilin Lyases in Synechococcus sp. PCC 7002

    … for chromophore (bilin) attachment to phycobiliproteins (light harvesting) in cyanobacteria. Candidates for these lyases were first identified in Fremyella diplosiphon as cpeS and cpeT. In Synechococcus sp. PCC 7002, there are three cpeS-like genes (named cpcS, cpcU, and cpcV) and one …

    uno Repository record for Identification and Characterization of a New Class of Bilin Lyases in Synechococcus sp. PCC 7002 (opens in a new tab)

  5. The Physiological Effects of Phycobilisome Antenna Modification on the Cyanobacterium Synechocystis sp. PCC 6803

    … core from which six rods radiate. The colored phycobiliproteins are held together by colorless linker polypeptides.</p><p>Several phycobilisome truncation mutants have been generated in Synechocystis 6803. The first, CB, has truncated phycobilisome rods; the second, CK, has only the …

    wustl Repository record for The Physiological Effects of Phycobilisome Antenna Modification on the Cyanobacterium Synechocystis sp. PCC 6803 (opens in a new tab)

  6. Lipidų ir fikobiliproteinų kiekiai gėlavandenių planktono melsvabakterių biomasėje, surinktoje vandens žydėjimų laikotarpiu /

    … of their quantity, the amounts of lipids and phycobiliproteins were determined in cyanobacteria biomass, the intervals of which varied with different intensities both between the same species of cyanobacteria dominating the biomass, and between different ones. Biomass analysis with a light …

    vilnius Repository record for Lipidų ir fikobiliproteinų kiekiai gėlavandenių planktono melsvabakterių biomasėje, surinktoje vandens žydėjimų laikotarpiu / (opens in a new tab)

  7. Flow Cytometric Analysis for Cyanobacteria in 36 New Jersey Freshwater Bodies

    … strategies. These microorganisms contain phycobiliproteins such as phycoerytrhin, and allophycocyanin as part of the phycobillisome that allow autofluorescence. In this study, 36 freshwater bodies from 14 New Jersey counties were collected and processed for flow cytometric analysis for …

    shu-thes Repository record for Flow Cytometric Analysis for Cyanobacteria in 36 New Jersey Freshwater Bodies (opens in a new tab)

  8. ISOLATION OF ELECTRON TRANSPORT COMPONENTS FROM MICROCYSTIS AERUGINOSA AND OSCILLATORIA SP

    … eluted much earlier than the main contaminant, phycobiliproteins. Plastocyanin was also well resolved from cytochrome c553, which possesses similar molecular weight and charge characteristics. It was therefore possible for the first time, to purify an acidic cynaobacterial plastocyanin to …

    nus Repository record for ISOLATION OF ELECTRON TRANSPORT COMPONENTS FROM MICROCYSTIS AERUGINOSA AND OSCILLATORIA SP (opens in a new tab)

  9. Characterization of Slr1098, a Protein with Similarity to the Bilin Lyase Subunit CpcE from the Cyanobacterium Synechocystis sp. PCC 6803

    The goal of this research is to investigate the role of the slr1098 gene in the cyanobacterium Synechocystis sp. PCC 6803, a gene with similarity to cpcE which encodes a subunit of an enzyme involved in bilin attachment to phycocyanin. This protein is hypothesized to be involved in oligomerization …

    uno Repository record for Characterization of Slr1098, a Protein with Similarity to the Bilin Lyase Subunit CpcE from the Cyanobacterium Synechocystis sp. PCC 6803 (opens in a new tab)

  10. Characterization of Enzymes Involved in Bilin Attachment to Allophycocyanin in the Cyanobacterium Synechococcus sp. PCC 7002

    The goal of this research is to identify and characterize enzymes involved in bilin attachment to the phycobiliprotein allophycocyanin in the cyanobacterium Synechococcus sp. PCC 7002. Candidates for lyases responsible for attachment of phycocyanobilin to allophycocyanin are two cpeS-like genes …

    uno Repository record for Characterization of Enzymes Involved in Bilin Attachment to Allophycocyanin in the Cyanobacterium Synechococcus sp. PCC 7002 (opens in a new tab)

  11. Techno-Economic Evaluation of a Commercial c-Phycocyanin Extraction Process

    … the development of natural pigment products from phycobiliproteins, a family of proteins found in cyanobacteria. One such phycobiliprotein is c-phycocyanin (cPC), a bright blue pigment that has already found widespread application in the food and pharmaceutical industries. It can also be used in …

    cape-town Repository record for Techno-Economic Evaluation of a Commercial c-Phycocyanin Extraction Process (opens in a new tab)