作者: R A Black , S R Kronheim , J E Merriam , C J March , T P Hopp
DOI: 10.1016/S0021-9258(18)83546-3
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摘要: Interleukin-1 beta is a 17.4-kilodalton hormone derived from 33-kilodalton inactive precursor produced by monocytes. We used the as substrate to detect proteolytic activities in peripheral blood mono-nuclear cell-conditioned medium that might be involved interleukin-1 processing. found conditioned medium, following passage through DEAE-Sephacel, generates biologically active fragment runs slightly higher than mature sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The responsible activity behaved single protein ion exchange chromatography. It was completely inhibited metal chelators and not inhibitors of serine, cysteine, or aspartate proteases, it dependent on both calcium (or magnesium) zinc. enzyme three substrate-based metalloprotease inhibitors, phosphoramidon, benzyloxycarbonyl-Gly-Leu-NH2, N-(2-carboxy-3-phenylpropionyl)-Leu. NH2-terminal sequence analysis showed cleavage occurred between histidine an residue, digestion synthetic peptides indicated protease specific for pre-aspartate cleavages.