FEBS Letters | |
Isolation and characterization of biliprotein aggregates from Acaryochloris marina, a Prochloron‐like prokaryote containing mainly chlorophyll d | |
Senger, Horst1  Mörschel, Erhard1  Miyachi, Shigetoh3  Miyashita, Hideaki2  Marquardt, Jürgen1  | |
[1] Fachbereich Biologie/Botanik, Philipps-Universität Marburg, Karl-von-Frisch-Strasse, D-35032 Marburg, Germany;Marine Biotechnology Institute, Kamaishi Laboratories, Kamaishi, Iwate 026, Japan;Marine Biotechnology Institute, Bukyo-ku, Tokyo 113, Japan | |
关键词: Phycobiliprotein; Allophycocyanin; Phycocyanin; Light harvesting antenna; Chlorophyll d; Prochlorophyte; (Acaryochloris marina); AP; allophycocyanin; Chl; chlorophyll; PAGE; polyacrylamide gel electrophoresis; PBS; phycobilisome; PC; phycocyanin; PE; phycoerythrin; SDS; sodium dodecyl sulfate; | |
DOI : 10.1016/S0014-5793(97)00631-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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