title: [Purification and partial biochemical characterization of the rabbit interleukin-1].
abstract: 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.
authors.forename: N D
authors.initials: ND
authors.lastname: Perumov
authors.forename: A S
authors.initials: AS
authors.lastname: Simbirtsev
authors.forename: E V
authors.initials: EV
authors.lastname: Mitrofanov
authors.forename: A K
authors.initials: AK
authors.lastname: Shishov
authors.forename: S A
authors.initials: SA
authors.lastname: Ketlinskiĭ
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007375:Interleukin-1 / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008970:Molecular Weight; D011817:Rabbits
chemical_list: D007375:Interleukin-1
vernacular_title: Ochistka i chastichnaia biokhimicheskaia kharakteristika interleĭkina-1 krolika.