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Biokhimiia ; 53(1): 25-30, 1988 Jan.
Article in Russian | MEDLINE | ID: mdl-3258760

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.


Subject(s)
Interleukin-1/isolation & purification , Animals , Chromatography, Gel , Chromatography, High Pressure Liquid , Electrophoresis, Polyacrylamide Gel , Isoelectric Focusing , Molecular Weight , Rabbits
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