Highly efficient purification of the 33-, 24-, and 18-kDa proteins in spinach photosystem II by butanol/water phase partitioning and high-performance liquid chromatography.
The 33-, 24-, and 18-kDa proteins involved in photosynthetic oxygen evolution were purified from spinach photosystem II particles by butanol/water phase partitioning and high-performance liquid chromatography with a silica-based cation-exchange column. With this procedure a significant improvement was made in the time required for the purification and also in the amount and purity of the proteins. The N-terminal sequence of amino acid was determined for the purified proteins. Partial degradation of the proteins, which sometimes occurred in the purification, was not detected in the new procedure.
Yamamoto
Y
Y
Nakayama
S
S
Cohn
C L
CL
Krogmann
D W
DW
D000596:Amino Acids / Q000032:analysis; D000440:Butanols; D002734:Chlorophyll / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D045342:Light-Harvesting Protein Complexes; D008970:Molecular Weight; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins / Q000302:isolation & purification*; D010944:Plants / Q000032:analysis*; D014867:Water
D000596:Amino Acids; D000440:Butanols; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D014867:Water; D002734:Chlorophyll