Abstract
Three chlorophyll-protein complexes of a Chroomonas species (Cryptophyceae) have been separated by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The two bands at 100 and 42 kDa are Complex I (CP I) and Complex IV (CP IV), the ubiquitous chlorophyll a-proteins associated with Photosystems I and II, respectively. The third 55 kDa band, which had two peptide subunits (24 and 20 kDa), contained both chlorophyll a and chlorophyll c2 in a molar ratio of 1.4 chlorophyll a to 1 chlorophyll c2 ( chlorophyll a chlorophyll c2 ratio in whole cells = 4). A chlorophyll a c2 fraction with similar spectral and electrophoretic properties was isolated by digitonin-sucrose density gradient centrifugation. This fraction had no photochemical activity and contained only a single carotenoid species with absorbance maxima in methanol at 424, 448 and 476 nm. Efficient energy transfer from chlorophyll c2 to chlorophyll a occurred in the complex.
Original language | English |
---|---|
Pages (from-to) | 310-319 |
Number of pages | 10 |
Journal | BBA - Bioenergetics |
Volume | 722 |
Issue number | 2 |
DOIs | |
Publication status | Published - 17 Feb 1983 |
Keywords
- (Cryptophyceae)
- Chlorophyll c
- Chlorophyll-protein
- Fluorescence
- Light-harvesting complex