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

1996; Elsevier BV; Volume: 1276; Issue: 2 Linguagem: Inglês

10.1016/0005-2728(96)00066-7

1879-2650

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

Glycosylation and Glycoproteins Research

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.