Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae
| Autor: | Roger G. Hiller, Pamela M. Wrench, Frank P. Sharples, Keli Ou |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Light-harvesting
Chlorophyll ved/biology.organism_classification_rank.species Ion chromatography Molecular Sequence Data Photosynthetic Reaction Center Complex Proteins Biophysics Light-Harvesting Protein Complexes Protozoan Proteins Transit sequence Biology Biochemistry Dinophyceae chemistry.chemical_compound Protein sequencing Amphidinium carterae Peridinin-chlorophyll a-protein Animals Amino Acid Sequence Peptide sequence chemistry.chemical_classification Molecular mass Base Sequence Sequence Homology Amino Acid ved/biology Chlorophyll A (Amphidinium carterae) Cell Biology Peridinin Carotenoids Amino acid Molecular Weight chemistry Dinoflagellida Sequence Analysis DNA |
| Zdroj: | Biochimica et biophysica acta. 1276(2) |
| ISSN: | 0006-3002 |
| Popis: | Peridinin-chlorophyll a-proteins (PCPs) have been purified by combination of ammonium sulphate precipitation and cation exchange chromatography. The amino acid sequences of several of the most abundant forms have been deduced by direct protein sequencing and from DNA and indicate a highly conserved multi-gene family. At least two of the PCP genes are tandemly arranged. A novel form of the protein was also obtained in low yield with fewer peridinins (six vs eight) per chlorophyll a and with a different molecular mass (34 kDa vs 32 kDa) of its apoprotein. It had only 31% sequence identity with any of the more abundant PCP forms but retained a two-domain structure. |
| Databáze: | OpenAIRE |
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