Abstract
Ion exchange chromatography of the haemolymph proteins of Malacosoma americanum and Rothschildia orizaba on DEAE cellulose, yielded 5 and 4 fractions respectively. The esterase activity of each fraction was estimated. In both cases each fraction was characterized by the presence of certain specific proteins which were detected as antigens by immunodiffusion in agar. Gel filtration on Sephadex G-200 of fractions obtained from ion exchange chromatography yielded antigenically pure proteins. Sedimentation constants and isoelectric points were obtained for a blue-green chromoprotein from M. americanum, and for the ‘common’ larval protein and ‘egg’ protein of R. orizaba.
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