PRELIMINARY INVESTIGATIONS INTO THE STRUCTURE AND ACTIVITY OF RIBULOSE BISPHOSPHATE CARBOXYLASE FROM TWO PHOTOSYNTHETIC DINOFLAGELLATES

PRELIMINARY INVESTIGATIONS INTO THE STRUCTURE AND ACTIVITY OF RIBULOSE BISPHOSPHATE CARBOXYLASE... ABSTRACT Ribulose bisphosphate carboxylase / oxygenase (Rubisco) from the dinoflagellates Symbiodinium sp. Freudenthal and Amphidinium carterae Hulburt rapidly loses activity following cell lysis. Evidence presented indicates that this is not due to proteolysis. Using the tight binding inhibitor (14C) carboxyarabinitol bisphosphate as a marker, the Rubisco large subunit (LSu) from Symbiodinium sp. was purified. The subunit molecular weight was 56 kDa, while non‐denaturing polyacrylamide gel electrophoresis indicated that the purified protein had a molecular weight significantly less than that expected of the intact hexadecameric protein. No trace of the small subunit was apparent. The initial loss of carboxylase activity following cell lysis may be due to instability of the quaternary structure of the enzyme. Antibodies prepared to the purified LSU cross‐reacted with LSus from other dinoflagellates but not with the LSus of higher plants, diatoms, and other chromophytic algae. This suggests that the LSu of at least some dinoflagellates is antigenically different from that of other eukaryotes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Phycology Wiley

PRELIMINARY INVESTIGATIONS INTO THE STRUCTURE AND ACTIVITY OF RIBULOSE BISPHOSPHATE CARBOXYLASE FROM TWO PHOTOSYNTHETIC DINOFLAGELLATES

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Abstract

ABSTRACT Ribulose bisphosphate carboxylase / oxygenase (Rubisco) from the dinoflagellates Symbiodinium sp. Freudenthal and Amphidinium carterae Hulburt rapidly loses activity following cell lysis. Evidence presented indicates that this is not due to proteolysis. Using the tight binding inhibitor (14C) carboxyarabinitol bisphosphate as a marker, the Rubisco large subunit (LSu) from Symbiodinium sp. was purified. The subunit molecular weight was 56 kDa, while non‐denaturing polyacrylamide gel electrophoresis indicated that the purified protein had a molecular weight significantly less than that expected of the intact hexadecameric protein. No trace of the small subunit was apparent. The initial loss of carboxylase activity following cell lysis may be due to instability of the quaternary structure of the enzyme. Antibodies prepared to the purified LSU cross‐reacted with LSus from other dinoflagellates but not with the LSus of higher plants, diatoms, and other chromophytic algae. This suggests that the LSu of at least some dinoflagellates is antigenically different from that of other eukaryotes.

Journal

Journal of PhycologyWiley

Published: Feb 1, 1995

References

  • Characterization of satellite DNA from three marine dinoflagellates (Dinophyceae): Glenodinium sp. and two members of the toxic genus, Protogonyaulax
    Boczar, Boczar; Liston, Liston; Cattolico, Cattolico
  • Activity ratios of ribulose‐1,5‐bisphosphate carboxylase accurately reflect carbamylation ratios
    Butz, Butz; Sharkey, Sharkey
  • Ribulose bisphosphate carboxylase from chlorophyll c ‐containing algae
    Plumley, Plumley; Kirchman, Kirchman; Hodson, Hodson; Schmidt, Schmidt
  • Photosynthetic carbon dioxide fixation in zooxanthellae
    Streamer, Streamer; McNeil, McNeil; Yellowlees, Yellowlees

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