Isolation and characterization of biliprotein aggregates from Acaryochloris marina, a Prochloron-like prokaryote containing mainly chlorophyll d.
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 x 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.
Marquardt
J
J
Fachbereich Biologie/Botanik, Philipps-Universität Marburg, Germany.
Senger
H
H
Miyashita
H
H
Miyachi
S
S
Mörschel
E
E
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D002734:Chlorophyll; D000458:Cyanobacteria / Q000737:chemistry*; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000648:ultrastructure; D010798:Phycocyanin / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D013050:Spectrometry, Fluorescence
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins; D010940:Plant Proteins; C002497:allophycocyanin; D010798:Phycocyanin; D002734:Chlorophyll; C107509:chlorophyll d