| 摘要 |
A previously undescribed Interleukin-6 inhibitor activity has been successfully isolated from the supernatant of the human promyelocytic leukemia cell line HL-60. Treatment of the HL-60 cell line with cycloheximide prevents the appearance of the inhibitory activity in the cellular supernatant. Incubation of the HL-60 supernatant with trypsin destroys the activity. The above observations indicate the inhibitor is a protein. Membrane and gel filtration studies indicate the protein has a molecular weight between 10,000 and 30,000 daltons. The inhibitor was partially isolated from other proteins by dye-ligand and reverse phase chromatography. |
