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Title Chromopeptides from phycoerythrins. Structure and linkage of a phycoerythrobilin tryptic tripeptide derived from a B-phycoerythrin
Creator/Author Schoenleber, R.W. ; Leung, S.L. ; Lundell, D.J. ; Glazer, A.N. ; Rapoport, H.
Publication Date1983 Jun 15
OSTI IdentifierOSTI ID: 5708517
Other Number(s)CODEN: JACSA
Resource TypeJournal Article
Resource RelationJ. Am. Chem. Soc. ; Vol/Issue: 105:12
Research OrgLawrence Berkeley Lab., CA
Subject400301 -- Organic Chemistry-- Chemical & Physicochemical Properties-- (-1987) ;550700 -- Microbiology; ;PEPTIDES-- STRUCTURAL CHEMICAL ANALYSIS; ABSORPTION SPECTRA;ALGAE;DIGESTION;ENZYME ACTIVITY;EXPERIMENTAL DATA;HEAVY WATER;LIQUID COLUMN CHROMATOGRAPHY;NMR SPECTRA;PIGMENTS;POLYPEPTIDES;SAMPLE PREPARATION;TRYPSIN
Related SubjectCHROMATOGRAPHY;DATA;ENZYMES;HYDROGEN COMPOUNDS;HYDROLASES;INFORMATION;NUMERICAL DATA;ORGANIC COMPOUNDS;OXYGEN COMPOUNDS;PEPTIDE HYDROLASES;PEPTIDES;PLANTS;PROTEINS;SEPARATION PROCESSES;SERINE PROTEINASES;SPECTRA;WATER
Description/Abstract Phycoerythrobilin peptides were prepared from Porphyridium cruentum B-phycoerythrin by tryptic digestion and isolated under mild conditions without alteration in the spectroscopic properties of the bilin.^High-resolution /sup 1/H NMR spectral analysis of the smallest trypsin fragment derived from the ..cap alpha.. subunit of B-phycoerythrin, the ..cap alpha../sub 1/-B-phycoerythrobilitripeptide (3), has provided direct proof that the bilin is linked to the peptide through a single bond, a thioether linkage at the 3`-position of ring A. Two linkages between the bilin and peptide have been proposed by others.^The present study confirms previous reports on the major structural features of the free phycoerythrobilin chromophore and indicates probable stereochemical assignments for all of the chiral centers.^5 figures, 2 tables.
Country of PublicationUnited States
LanguageEnglish
FormatPages: 4072-4076
System Entry Date2001 May 13

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