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Isolation of allophycocyanin B from Rhodella violacea results in a model of the core from hemidiscoidal phycobilisomes of rhodophyceae
Author(s) -
Reuter Wolfgang,
Nickel Claudia,
Wehrmeyer Werner
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81073-w
Subject(s) - phycobilisome , allophycocyanin , fluorescence , linker , phycocyanin , chemistry , microbiology and biotechnology , biochemistry , biology , biophysics , cyanobacteria , genetics , bacteria , optics , computer science , operating system , physics
Two ‘trimeric’ allophycocyanin complexes could be isolated from the hemidiscoidal phycobilisomes of Rhodella violacea , AP = (α ∗Ap α 2 AP β 2 AP β ∗AP ) and APB = (α ∗Ap α AP α APB β 2 AP β ∗AP ) · L c 13.5APB . The isolation was performed by combined methods of gradient centrifugation, hydroxylapatite chromatography and ‘native’ polyacrylamide gel electrophoresis. AP showed the well‐known spectral characteristics of allophycocyanin without linker polypeptide. APB is characterized by its long wavelength absorbing shoulder (675 nm) and fluorescence emission (682nm), respectively. The existence of two low molecular linker polypeptides L c 12.5 and L c 13.5APB in the phycobilisomes of Rhodella violacea , their stoichiometric calculations and the localization of L c 13.5APB in allophycocyanin B facilitated the construction of a model of the phycobilisome core.