Williams, Richard Stephen (1987) Studies on the peripheral light-harvesting chlorophyll-protein complex of photosystem I in "Pisum sativum L.". PhD thesis, University of Warwick.

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Abstract

Two novel sub-thylakoid fractions from Pisum sativum L. containing the photosystem I reaction centre and peripheral light-harvesting complex were characterised. Both preparations displayed a number of spectral and biochemical properties in common with those exhibited by a standard photosystem I preparation. However, both differed markedly in their sedimentation properties when compared with the standard preparation.

In addition, one of the novel preparations was found to contain large amounts of the chlorophyll a/b-binding light-harvesting complex of photosystem II (LHC II). It was shown that excitation energy is transferred from the LHC II component to the photosystem I component within this preparation. Such excitation energy transfer has not previously been demonstrated in a sub- thylakoid preparation.

Monoclonal and polyclonal antibodies were raised to the apoproteins of the chlorophyll a/b-binding peripheral light-harvesting complex of photosystem I (LHC I). Assays of polyclonal antibody specificity showed immunological cross-reaction between individual LHC I apoproteins and between the apoproteins of the LHC I and LHC II.

The immunological cross-reactivity between the polypeptides of the LHC I and LHC II were shown to be spurious. The LHC I apoproteins were found to fall into two distinct immunological groupings which were supported by assays of monoclonal antibody specificity and by a comparison of their partial peptide maps.

Immunoblot assays showed that the LHC I apoproteins failed to accumulate in the thylakoid membrane under intern intermittent illumination. When greening pea seedlings were placed in the dark, the LHC I apoproteins not only failed to accumulate but underwent a net loss during the dark period. In vivo radiolabelling experiments showed that the apoproteins of the LHC I continued to be synthesised even after 16 h darkness. The failure of these proteins to accumulate in the thylakoid in the dark is therefore due to protein turnover.

Item Type:	Thesis or Dissertation (PhD)
Subjects:	Q Science > QD Chemistry Q Science > QK Botany
Library of Congress Subject Headings (LCSH):	Peas -- Analysis, Chlorophyll -- Synthesis, Proteins -- Analysis
Official Date:	March 1987
Dates:	Date Event March 1987 UNSPECIFIED
Institution:	University of Warwick
Theses Department:	Department of Biological Sciences
Thesis Type:	PhD
Publication Status:	Unpublished
Supervisor(s)/Advisor:	Ellis, R. J. (Reginald John)
Sponsors:	Science and Engineering Research Council (Great Britain)
Extent:	xxi, 394 leaves : illustrations
Language:	eng

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