[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.
Perumov
N D
ND
Simbirtsev
A S
AS
Mitrofanov
E V
EV
Shishov
A K
AK
Ketlinskiĭ
S A
SA
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
D007375:Interleukin-1
Ochistka i chastichnaia biokhimicheskaia kharakteristika interleĭkina-1 krolika.