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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1984-6-14
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pubmed:abstractText |
A bilin-containing fragment of the beta subunit of Porphyridium cruentum B-phycoerythrin produced by cleavage with thermolysin was shown by sequence analysis (Lundell, D.J., Glazer, A.N., DeLange, R.J., and Brown, D.M. (1984) J. Biol. Chem. 259, 5472-5480) to have the following structure. (Formula: see text) Secondary ion mass spectrometry of this bilin-peptide yielded a protonated molecular ion of 1629 mass units corresponding to that predicted from the composition of the fragment, and indicated that the heptapeptide is linked to ring A and the tripeptide to ring D. NMR spectra provided definitive evidence for a thioether linkage at the C-3' carbon of ring A and a second thioether linkage at teh C-18' carbon of ring D of the bilin. This is the first documented report of a bilin linked through two thioether linkages to a polypeptide.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bile Pigments,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phycoerythrin,
http://linkedlifedata.com/resource/pubmed/chemical/Pigments, Biological,
http://linkedlifedata.com/resource/pubmed/chemical/Thermolysin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5481-4
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:6715354-Amino Acid Sequence,
pubmed-meshheading:6715354-Bile Pigments,
pubmed-meshheading:6715354-Macromolecular Substances,
pubmed-meshheading:6715354-Magnetic Resonance Spectroscopy,
pubmed-meshheading:6715354-Mass Spectrometry,
pubmed-meshheading:6715354-Peptide Fragments,
pubmed-meshheading:6715354-Phycoerythrin,
pubmed-meshheading:6715354-Pigments, Biological,
pubmed-meshheading:6715354-Protein Binding,
pubmed-meshheading:6715354-Rhodophyta,
pubmed-meshheading:6715354-Thermolysin
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pubmed:year |
1984
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pubmed:articleTitle |
Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Structural studies on a doubly peptide-linked phycoerythrobilin.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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