J. Biol. Chem., Vol. 259, Issue 9, 5485-5489, May, 1984
Bilin attachment sites in the alpha and beta subunits of B- phycoerythrin. Structural studies on the singly linked phycoerythrobilins
RW Schoenleber, DJ Lundell, AN Glazer and H Rapoport
Five unique phycoerythrobilin (PEB) peptides were prepared from
Porphyridium cruentum B-phycoerythrin by a combination of tryptic and
thermolytic digestion without alteration in the spectroscopic properties of
the bilin (Lundell, D.J., Glazer, A.N., DeLange, R.J., and Brown, D.M.
(1984) J. Biol. Chem. 259, 5472-5480). alpha-1 Cys(PEB)- Tyr-Arg alpha-2
Leu-Cys(PEB)-Val-Pro-Arg beta-1 Met-Ala-Ala-Cys(PEB)- Leu-Arg beta-2T
Phe-Ala-Ala-Gly-Asp-Cys(PEB)-Thr-Ser (Formula: see text) where alpha and
beta refer to the subunits from which the peptides were derived High
resolution 1H NMR analysis of peptides alpha- 2, beta-1, and beta-2T
combined with earlier studies of peptide alpha-1 (Schoenleber, R.W., Leung,
S.-L., Lundell, D.J., Glazer, A.N., and Rapoport, H. (1983) J. Am. Chem.
Soc. 105, 4072-4076) 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. The circular dichroism spectra of the four singly linked
PEB peptides show that the configuration at C-16 is R in each instance. The
present study coupled with previously reported results on peptide beta-3T
(Schoenleber, R.W., Lundell, D.J., Glazer, A.N., Rapoport, H. (1984) J.
Biol. Chem. 259, 5481-5484 provides the first comprehensive analysis of the
structure of all the polypeptide-linked prosthetic groups on the alpha and
beta subunits of B-phycoerythrin.
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