Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1984-6-14
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5481-4
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Structural studies on a doubly peptide-linked phycoerythrobilin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.