Abstract: There is disclosed an isolated polypeptide and derivatives thereof having protease biological activity for human precursor IL-1? and for a substrate comprising: R1—Asp—R2—R3 wherein R1 and R3 are independently any D or L isomer amino acid, R2 is Ala or Gly, and wherein the specific protease cleavage site is between Asp and R2. Inhibitor compounds, compositions and methods for inhibiting Interleukin 1? protease activity are also disclosed. The inhibitor compounds comprise an amino acid sequence of from 1 to about 5 amino acids having an N-terminal blocking group and a C-terminal Asp residue connected to an electronegative leaving group, wherein the amino acid sequence corresponds to the sequence Ala-Tyr-Val-His-Asp.

Abstract: There is disclosed an isolated polypeptide and derivatives thereof having protease biological activity for human precursor IL-1.beta. and for a substrate comprising:R.sub.1 -Asp-R.sub.2 -R.sub.3wherein R.sub.1 and R.sub.3 are independently any D or L isomer amino acid, R.sub.2 is Ala or Gly, and wherein the specific protease cleavage site is between Asp and R.sub.2. Inhibitor compounds, compositions and methods for inhibiting Interleukin 1.beta. protease activity are also disclosed. The inhibitor compounds comprise an amino acid sequence of from 1 to about 5 amino acids having an N-terminal blocking group and a C-terminal Asp residue connected to an electronegative leaving group, wherein the amino acid sequence corresponds to the sequence Ala-Tyr-Val-His-Asp.

Abstract: There is disclosed an isolated polypeptide and derivatives thereof having protease biological activity for human precursor IL-1.beta. and for a substrate comprising:R.sub.1 -Asp-R.sub.2 -R.sub.3wherein R.sub.1 and R.sub.3 are independently any D or L isomer amino acid, R.sub.2 is Ala or Gly, and wherein the specific protease cleavage site is between Asp and R.sub.2. Inhibitor compounds, compositions and methods for inhibiting Interleukin 1.beta. protease activity are also disclosed. The inhibitor compounds comprise an amino acid sequence of from 1 to about 5 amino acids having an N-terminal blocking group and a C-terminal Asp residue connected to an electronegative leaving group, wherein the amino acid sequence corresponds to the sequence Ala-Tyr-Val-His-Asp.

Abstract: Interleukin 1 has been purified by use of various techniques including ion exchange chromatography and dye-ligand affinity chromatography. By these techniques, interleukin 1 has been purified to homogeneity. The high purification of interleukin 1 has enabled the amino acid composition of this protein to be ascertained and its amino acid sequence to be partially determined.

Abstract: There is disclosed an isolated polypeptide and derivatives thereof having protease biological activity for human precursor IL-1.beta. and for a substrate comprising:R.sub.1 - Asp - R .sub.2 - R.sub.3wherein R.sub.1 and R.sub.3 are independently any D or L isomer amino acid, R.sub.2 is Ala or Gly, and wherein the specific protease cleavage site is between Asp and R.sub.2. Inhibitor compounds, compositions and methods for inhibiting Interleukin 1.beta. protease activity are also disclosed. The inhibitor compounds comprise an amino acid sequence of from 1 to about 5 amino acids having an N-terminal blocking group and a C-terminal Asp residue connected to an electronegative leaving group, wherein the amino acid sequence corresponds to the sequence Ala-Tyr-Val-His-Asp.

Abstract: Double-stranded cDNA is prepared from polyadenylated RNA extracted from activated human peripheral blood adherent mononuclear cells. The cDNA is inserted within a plasmid vector and then the recombinant plasmid employed to transform an appropriate host. Transformed hosts are identified and grouped into pools. Plasmid DNA prepared from these pools is hybridized with a labeled, synthetic oligonucleotide probe corresponding to a portion of the amino acid sequence of the interleukin 1 protein. Pools of host cells that provide a positive signal to the probe are identified, plated out and then employed in direct bacterial colony hybridization with the same probe, thereby to isolate the particular positive colony. Plasmid DNA is prepared from this colony and characterized by restriction enzyme mapping and sequencing by chain-termination method. The coding region for the IL-1 gene is inserted into a shuttle vector for amplification of the vector followed by expression of functional IL-1.

Abstract: A process is provided for purifying recombinant IL-1 from microbial cells, comprising suspending the cells in an aqueous buffered medium having a pH from about 1 to about 5; disrupting the cells to provide an extract containing solubilized IL-1; and recovering solubilized Il-1 from the extract.