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No description available.

Dinoflagellates are a diverse group of protists, some of which are photosynthetic. The typical dinoflagellate chloroplast contains two proteins not found in any other photosynthetic eukaryote: peridinin-chlorophyll a-protein (PCP) and Form II ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). / Immunoelectron microscopic observations on the dinoflagellate Amphidinium carterae show that PCP is localized in the chloroplast stroma, not in the thylakoid lumen as previously postulated due to the presence of a putative lumen-targeting sequence. / Antisera against Form II Rubisco from bacterial (Rhodospirillum rubrum) and dinoflagellate (Symbiodinium sp.) sources were both shown to label the chloroplast and pyrenoid of A. carterae . Antiserum to Form I Rubisco from the haptophyte, alga Isochrysis galbana resulted in no labelling. Parallel experiments on the dinoflagellate Peridinium foliaceum, whose chloroplasts are all attributed to its diatom endosyrnbiont and on the diatom Phaeodactylum tricornutum revealed plastid pyrenoid labelling only with antiserum to Form I Rubisco.

The technique of protein A-gold immunoelectron microscopy was used to determine the distributions of two photosynthetic complexes in the thylakoid membranes of the diatom Phaeodactylum tricornutum. The fucoxanthin-chlorophyll a/c light-harvesting complex, believed to be associated with photosystem II, was found to be equally distributed among appressed and unappressed membranes, whereas photosystem I was slightly more concentrated in the latter. These results suggest that in diatoms, the two photosystems and their associated light-harvesting complexes are essentially equally distributed on the two types of membranes, in marked contrast to the lateral heterogeneity observed in higher plants and green algae. Furthermore, it was expected that in P. tricornutum, the nuclear-coded proteins of the fucoxanthin-chlorophyll a/c light-harvesting complex would be present in the vesicles of the periplastidal reticulum, which were postulated to be involved in protein transport into chloroplasts. Immunolabelling results, however, indicated that these proteins were absent from the periplastidal vesicles.

Typescript (photocopy) / 116, 14 leaves, [5] leaves of plates : ill. ; 30 cm. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Thesis (Ph.D.) Dept. of Botany, University of Adelaide, 1982

133 leaves : graphs, tables ; 30 cm. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Thesis (Ph.D.)--University of Adelaide, Dept. of Botany, 1978

Typescript (photocopy) / 116, 14 leaves, [5] leaves of plates : ill. ; 30 cm. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Thesis (Ph.D.) Dept. of Botany, University of Adelaide, 1982

Thesis (Ph.D.) Dept. of Botany, University of Adelaide, 1982. / Typescript (photocopy).

Thesis (Ph.D.) -- University of Adelaide, Department of Botany, 1978.

Thesis (B.Sc.(Hons.))--University of Adelaide, Dept. of Botany, 1973. Deposited in accordance with the rules applying to the award of the John Bagot Medal.