Sequences of the N-terminus portions of biliproteins

Abstract

The N-terminal sequences of the separated polypeptide chains of biliproteins isolated from several Cyanophyta, Rhodophyta, and Cryptophyta have been determined. The portions of the sequences determined for theα (fast) chain of C-phycocyanin from both procaryotic and eucaryotic cells are extremely conservative. Methionine is the N-terminal amino acid in most of the species studied. The N-terminus and subsequent sequence of phycoerythrinα chains are almost identical with those of the C-phycocyaninβ chain. Theβ (slow) chain of C-phycocyanin is also rather conservative in amino acid substitution but has more variation than theα chain. The variations are consistent with single base changes in codons and conserve the size and functional characteristics of the amino acid. The sequence homologies are consistent with the phylogenetic relationship between Cyanophyta and the chloroplast of Rhodophyta. There are no other reported sequences of polypeptide chains of the same or related proteins from such different strains of microorganisms that show such close sequence homology.