Examination of cottonseed protein in the ultracentrifuge has revealed the presence of at least four sedimenting components with sedimentation constants of 18, 13, 8 and ∼2 Svedberg units. Ammonium sulphate fractionation failed to purify these components. Purification of the s13 and s8 components was achieved by the fractionation method of Karon et alia. No dissociation‐association reactions of the purified components were observed with changes in ionic strength in the range 0.1 to 0.5 or with changes in pH in the range 8–10.