One-step purification of functional light-harvesting 2 complex from Rhodobacter sphaeroides.
Most common method for isolation of light-harvesting 2 complex (LH2) is very time-consuming. In our present work functional LH2 complex was one-step rapidly purified from Rhodobacter sphaeroides by metal-ion affinity chromatography. The purified LH2 complex exhibited high activity in light absorption and energy transfer. Our present work provides an efficient approach for preparation of functional LH2 complex.
Zhao
Zhiping
Z
Key Laboratory of Biorheological Science and Technology (Chongqing University), Ministry of Education, Bioengineering College, Chongqing University, Chongqing 400044, People's Republic of China.
Hu
Zongli
Z
Liang
Yan
Y
Hu
Tingzhang
T
Tu
Yun
Y
Chen
Guoping
G
D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002852:Chromatography, Ion Exchange / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D045342:Light-Harvesting Protein Complexes / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*; D017830:Octoxynol / Q000737:chemistry; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D012242:Rhodobacter sphaeroides / Q000235:genetics / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D011994:Recombinant Proteins; D017830:Octoxynol