Abstract
A chlorophyll ac-fucoxanthin light-harvesting protein has been separated by SDS-polyacrylamide gel electrophoresis and by digitonin-sucrose density centrifigation from thylakoids of Pavlova lutherii. It contains a single major polypeptide of 21 kDa, comprises 69% of the total chlorophyll a and is enriched in chlorophyll c compared to the thylakoids. Energy transfer from chlorophyll c and fucoxanthin to chlorophyll a was demonstrated within the protein complex. Antibodies to the 21 kDa apoprotein showed cross-reactivity with the 26-28 kDa apoproteins of higher plant light-harvesting chlorophyll a b protein and with the 19 kDa apoprotein of the light-harvesting complex of diatoms, but much reduced or no cross-reactivity with the major thylakoid polypeptides of dinoflagellates and cryptophytes.
Original language | English |
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Pages (from-to) | 223-231 |
Number of pages | 9 |
Journal | BBA - Bioenergetics |
Volume | 932 |
Issue number | C |
DOIs | |
Publication status | Published - 1988 |
Keywords
- (P. lutherii)
- (Prymnesiophyta)
- chlorophyll c
- chlorophyll protein complex
- fucoxanthin
- light harvesting complex