Purification method for proteins.

摘要

Tumor necrosis factor (TNF) may be purified using a hydrophobic support in a chromatographic column that is then developed, preferably using high pressure liquid chromatography. Also, recombinantly produced biologically active proteins may be purified by passing a solution containing the protein through a continuous porous hydrophobic membrane, and recovering the fraction enriched in the desired protein. TNF and recombinant ricin toxin A chain may be purified. A highly purified TNF comprising at least 95% TNF, as determined by SDS-PAGE analysis, with an endotoxin content of less than 0.1 nm/mg TNF that is substantially free of pyrogens by the USP rabbit pyrogen test at a dosage range of 1.0 to 2.4 x 10<5> U/Kg is obtained.