ABSTRACTA protein isolate was prepared from edible beef plasma by complexing the proteins with sodium hexametaphosphate. The isolate contained 82 protein which was completely soluble within the pH range 5.0–8.0. Foam volumes of solutions of the phosphated protein was greater than those observed in egg albumen or in plasma proteins prepared by the ultrafiltration process. Electrophoretic resolution revealed small differences in the protein species in phosphated plasma isolates and that prepared by ultrafiltration. Amino acid analyses revealed no major difference between the two plasma protein isolates; the major difference was a reduced tryptophan content in the phosphated protei
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