Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae

Frank P. Sharples, Pamela M. Wrench, Keli Ou, Roger G. Hiller*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

62 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)117-123
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number2
Publication statusPublished - 12 Sep 1996


  • (Amphidinium carterae)
  • Amino acid sequence
  • Dinophyceae
  • Light-harvesting
  • Peridinin
  • Peridinin-chlorophyll a-protein
  • Transit sequence


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