Two anionic species of human IL-1 have been purified to homogeneity. These molecules were characterized as having pI of 5.4 and 5.2 and molecular weights identical to IL-1/6.8 (17,500). The specific activities of IL-1/5.4 and IL-1/5.2, as measured in the mouse thymocyte co-mitogenic assay, were identical to that of IL-1/6.8, namely 1.2 X 10(7) U/mg, with half-maximal stimulation observed at 2 X 10(-11) M. IL-1/5.4 and IL-1/5.2 were found to be antigenically distinct from IL-1/6.8 in an ELISA. IL-1/5.4 was structurally distinct from IL-1/6.8 based on reverse-phase HPLC or CNBr peptides. Intact IL-1/5.2 and three intact CNBr peptides of IL-1/5.4 were sequenced, with the identification of 74 amino acid residues. These sequences were found to correspond exactly with the amino acid sequence deduced from the IL-1-alpha cDNA reported by March et al.
Purification to homogeneity and amino acid sequence analysis of two anionic species of human interleukin 1.
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P M Cameron, G A Limjuco, J Chin, L Silberstein, J A Schmidt; Purification to homogeneity and amino acid sequence analysis of two anionic species of human interleukin 1.. J Exp Med 1 July 1986; 164 (1): 237–250. doi: https://doi.org/10.1084/jem.164.1.237
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