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Isolation and characterization of biliprotein aggregates from Acaryochloris marina, a Prochloron ‐like prokaryote containing mainly chlorophyll d
Author(s) -
Marquardt Jürgen,
Senger Horst,
Miyashita Hideaki,
Miyachi Shigetoh,
Mörschel Erhard
Publication year - 1997
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/s0014-5793(97)00631-5
Subject(s) - allophycocyanin , phycocyanin , phycobiliprotein , chemistry , prokaryote , phycoerythrin , pigment , cyanobacteria , biochemistry , biology , bacteria , organic chemistry , genetics , flow cytometry , gene
Phycobiliprotein aggregates were isolated from the prokaryote Acaryochloris marina , containing chlorophyll d as major pigment. In the electron microscope the biliprotein aggregates appear as rod‐shaped structures of 26.0×11.3 nm, composed of four ring‐shaped subunits 5.8 nm thick and 11.7 nm in diameter. Spectral data indicate that the aggregates contain two types of biliproteins: phycocyanin and an allophycocyanin‐type pigment, with very efficient energy transfer from the phycocyanin‐ to allophycocyanin‐type constituent. The chromophore‐binding polypeptides of the pigments have apparent molecular masses of 16.2 and 17.4 kDa. They crossreact with antibodies against phycocyanin and allophycocyanin from a red alga.

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