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Showing 1 to 6 of 6 for “"Allophycocyanin"”.

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

    … 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 termed cpcS and cpcU, and one cpeT-like gene termed cpcT. In vitro bilin …

    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)

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

    … 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 forward- scatter, phcyoerthrin and …

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

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

    … both apo- and holo-phycocyanin, but not to apo-allophycocyanin. Slr1098 blocked bilin addition at Cys-82 on CpcB by the CpcS/CpcU bilin lyase. Size exclusion chromatography and sucrose density gradient analysis of complexes formed suggest that Slr1098 strongly interacts with all intermediate …

    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)

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

    … system efficiently produced chromophorylated allophycocyanin (ApcA/ApcB), -phycocyanin, and -phycocyanin. This system was used to demonstrate that CpcS-I and CpcU proteins are both required attaching PCB to allophycocyanin subunits ApcD (AP-B) and ApcF (18). The N-terminal, AP-like domain …

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

  5. Pigment orientation changes detected by low temperature linear dichroism spectroscopy: cold-hardening transition in phycobilisome-containing organisms

    … to state 2 resulted in an increase in core allophycocyanin absorption parallel to the membrane, and a decrease in rod phycocyanin parallel absorption. This result supports the "spillover" and "PBS detachment" models of the light state transition in PBS-containing organisms, but not the …

    brock Repository record for Pigment orientation changes detected by low temperature linear dichroism spectroscopy: cold-hardening transition in phycobilisome-containing organisms (opens in a new tab)

  6. Lanthanides and quantum dots : time-resolved laser spectroscopy of biochemical Förster Resonance Energy Transfer (FRET) systems

    … acceptors, the luminescent crosslinked protein allophycocyanin (APC) and a commercial fluorescence dye (DY633), are investigated for direct comparison. FRET is demonstrated for all donor-acceptor pairs by acceptor emission sensitization and a more than 1000-fold increase of the luminescence …

    potsdam-diss Repository record for Lanthanides and quantum dots : time-resolved laser spectroscopy of biochemical Förster Resonance Energy Transfer (FRET) systems (opens in a new tab)