[Purification and partial biochemical characterization of the rabbit interleukin-1]

Rabbit interleukin-1 produced by peritoneal macrophages has been purified and partly characterized. The molecular mass of the protein as determined by gel filtration and SDS-PAAG electrophoresis is about 16-17 kD. The isoelectric points of interleukin-1 are as follows: 5.00, 6.75, 7.65, 8.75. A minor peptide possessing the interleukin-1 activity whose molecular mass determined by high performance liquid chromatography gel filtration is about 1500-3000 Da has also been discovered.