Human spleen cysteineproteinase inhibitor

摘要: Abstract The papain inhibitor from human spleen was purified by extraction in isotonic sucrose, acetone fractionation, papain-Sepharose affinity chromatography and gel filtration on Sephadex G-50. fractionated electrofocusing into four major isoelectric variants with pI values of 4.7, 5.0, 6.0 6.5. These can be classified two groups: the acidic type, comprising 4.7 neutral following properties distinguish types: 1. Immunological properties: antibodies raised against either precipitated both these, but not variants. antiserum epidermal cysteineproteinase variants, 2. Molecular size: two-dimensional electrophoresis gave molecular weights 11 400 for 12 000 variant contained compounds 800. 3. Enzyme spectrum: cathepsin B inhibited while type a poor inhibitor. Both types H, papain, ficin bromelain, although inhibition bromelain did exceed 70%. Human D, bovine trypsin chymotrypsin porcine elastase were type.