Purification to Homogeneity of Biologically Active Human Interleukin 1

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Abstract
Human interleukin 1 (IL-1) produced by lipopolysaccharide-stimulted monocytes was purified to homogeneity with retention of biological activity. IL-1 was measured by its ability to enhance the prolifertive response of thymocytes to phytohemagglutinin. The purification procedure included hydrophobic affinity chromatography on phenyl Sepharose, gel filtration through Ultrogel AcA54 and preparative isoelectric focusing. Both charged species of IL-1, pI 5.1 and 6.8 have a Mw of 14,500 as determined by sodium dodecylsulfate polyacrylamide gel electrophoresis. The complete purification resulted in a recovery of .apprx. 0.01% of IL-1 protein and if protection against losses by denaturation and adsorption in the final purification step was provided by bovine serum albumin, .apprx. 11% of IL-1 activity can be recovered.