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Open AccessJournal ArticleDOI

Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Structural studies on the singly linked phycoerythrobilins.

R W Schoenleber, +3 more
- 10 May 1984 - 
- Vol. 259, Iss: 9, pp 5485-5489
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TLDR
The present study coupled with previously reported results on peptide beta-3T has provided proof that all of the singly linked PEB peptides contain a thioether bond to the 3' position of ring A, and strong evidence in support of a trans-dihydro ring A in each of these chromopeptides.
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This article is published in Journal of Biological Chemistry.The article was published on 1984-05-10 and is currently open access. It has received 33 citations till now.

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Citations
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Book ChapterDOI

Phycobilisome and Phycobiliprotein Structures

TL;DR: Phycobilisomes serve as the primary light-harvesting antennae for Photosystem II in cyanobacteria and red algae and contain smaller amounts ‘linker polypeptides,’ most of which do not bear chromophores.
Journal ArticleDOI

Structure and function of light‐harvesting complexes and their polypeptides

TL;DR: In this article, a detailed biochemical and structural characterization of the pigment protein complexes of light harvesting antennae was obtained. And the detailed biochemical analysis also allowed a better identification of the various pigmentprotein complexes, which is essential for their isolation.
Journal ArticleDOI

Extraction and purification of C-phycocyanin from Spirulina platensis (CCC540).

TL;DR: In this study a simple protocol was developed for purifying phycocyanin (PC) from Spirulina platensis by using ammonium sulphate precipitation, followed by a single step chromatography by using DEAE-Cellulose-11 and acetate buffer.
Journal ArticleDOI

Characterization of the bilin attachment sites in R-phycoerythrin.

TL;DR: The availability of small bilin peptides was exploited to obtain more accurate molar extinction coefficients for peptide-linked PEB and PUB groups, and application of these extinction coefficients in the calculation of the bilin content of R-, B-, and C-phycoerythrins shows that there are 5 bilins/alpha beta in each of these three biliprotein types.
References
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Journal ArticleDOI

Subunit structure and chromophore composition of rhodophytan phycoerythrins. Porphyridium cruentum B-phycoerythrin and b-phycoerythrin.

TL;DR: In this paper, a comparative study of the two phycoerythrins of the unicellular red alga Porphyridium cruentum is presented, and it is shown that the presence and amount of phycourobilin chromophores in the native protein is correlated with the presence of the gamma subunit.
Journal ArticleDOI

Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies.

TL;DR: Comparison of the sequences from B-phycoerythrin to sequences of several other biliproteins has revealed the presence of a number of invariant tyrosyl and arginyl residues near bilin attachment sites.
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