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Structural studies on phycobiliproteins III. Comparison of bilin-containing peptides from the beta subunits of C-phycocyanin, R-phycocyanin, and phycoerythrocyanin.

Year: 1978

Type: article

Abstract: Pure bilin-containing peptides were isolated from the /l subunits of Porphyridium aerugineum C-phycocyanin, Porphyridium cruentum R-phycocyanin, and Anabaena uariabilis phycoerythrocyanin after cleavage with cyanogen bromide.The /3 subunits of C-phycocyanin and phycoerythrocyanin each carry two phycocyanobilin prosthetic groups, while the j3 subunit of R-phycocyanin carries one phycocyanobilin and one phycoerythrobilin.Both bilin peptides were isolated from C-and R-phycocyanin, but only one was purified from phycoerythrocyanin.In each case, as found for Synechococcus sp.6301 C-phycocyanin (Williams, V. P., and Glazer, A. N. ( 1978) J. Biol.Chem.253, ZOZ-2111, one of the bilin peptides represented the COOH-terminal region of the /3 subunit.The sequences of the bilin peptides from the /3 subunit of Synechococcus sp.C-phycocyanin (I) are compared with those of P. aerugineum C-phycocyanin (II), R-phycocyanin (III), and phycoerythrocyanin (IV):

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(17)38291-1

Authors: D.A. Bryant, C.S. Hixson, A.N. Glazer

Institutions: Institut Pasteur, University of California, Los Angeles, University of Washington, University of California, Berkeley

Language: English

Topic: Photosynthetic Processes and Mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1596496914

FWCI: 2.629

Cites: 19

Cited by: 52

Related to: 10