Use of adsorption chromatography on sephacryl S-500 for improved separation of isoforms of soluble photosynthetic catalysts from cyanobacteria

Abstract

Sphacryl S-500, a gel-filtration matrix, adsorbs water soluble proteins at high concentrations of ammonium sulfate. It has been used here as a matrix for adsorption chromatography, separating isoforms of cytochrome c553 and ferredoxin from Oscillatoria sp. and Microcystis aeruginosa, respectively. The isoforms of these proteins were separated at 35% and 40% saturated ammonium sulfate, respectively. Using this adsorption chromatography, we have purifield high levels of individual isoforms with improved resolution over conventional procedures such as polyacrylamide gel electrophoresis and ion-exchange chromatography.