title: 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.
abstract: 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.
authors.forename: Y
authors.initials: Y
authors.lastname: Yamamoto
authors.forename: S
authors.initials: S
authors.lastname: Nakayama
authors.forename: C L
authors.initials: CL
authors.lastname: Cohn
authors.forename: D W
authors.initials: DW
authors.lastname: Krogmann
mesh_terms: 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
chemical_list: 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