Abstract
The molecular properties of C-phycocyanin isolated from wild-type cells of the blue-green alga Oscillatoria agardhii are described as evaluated after final purification by polyacrylamide disc electrophoresis. The protein was found to consist of two polypeptide chains with methionine as the amino-terminal amino acid in both chains. The chains are connected with a disulfide bridge, and both contain at least one chromophore group per chain. The complete amino acid composition of each chain was determined by enzymic as well as acidic hydrolysis. Based on the presence of one phycocyanobilin for each chain, the molecular weights of 12 200 and 14 100 were obtained for the two chains. The amino acid composition, the peptide maps and amino-terminal sequence of the two chains revealed that they are similar in structure.
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