Purification and characterization of human recombinant interleukin-1 beta

A human interleukin-1 (IL-1) beta cDNA was cloned, and the region coding for the mature protein was expressed in Escherichia coli. The 17-kDa biologically active product was purified in 40% yield to apparent homogeneity, without chaotropes, from the soluble fraction of sonicated cell lysates. The re...

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Veröffentlicht in:	The Journal of biological chemistry 1987-08, Vol.262 (23), p.11176-11181
Hauptverfasser:	Meyers, C A, Johanson, K O, Miles, L M, McDevitt, P J, Simon, P L, Webb, R L, Chen, M J, Holskin, B P, Lillquist, J S, Young, P R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - analysis Analysis of the immune response. Humoral and cellular immunity Animals Biological and medical sciences Biological Assay Chromatography cloning Electrophoresis, Polyacrylamide Gel Escherichia coli Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Fundamental immunology gene expression Humans Immunobiology interleukin 1 Interleukin-1 - biosynthesis Interleukin-1 - genetics Interleukin-1 - isolation & purification Lymphokines, interleukins ( function, expression) Mice Mitosis Molecular Weight Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Regulatory factors and their cellular receptors Sulfhydryl Compounds - analysis T-Lymphocytes - cytology
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