Abstract
AbstractA low‐molecular‐weight proteinase inhibitor which has a molecular mass of 2,200 daltons was recently isolated from human epidermis. The isolated fraction demonstrated one protein band; when it was preincubated with papain, no band corresponding to products from the inhibitor was demonstrated in sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE). The isolated fraction was found to be immunologically distinct from a2 macroglobulin (α2‐M) by a double immunodiffusion test using anti‐α2‐M serum.The inhibitor possesses inhibitory activity against papain and bromelain, which are cysteine proteinases, plasmin and trypsin, serine proteinases, and collagenase, a metallo proteinase; however, it did not react with pepsin and cathepsin D, carboxyl proteinases. The inhibitor blocked papain and bromelain strongly, but trypsin, plasmin and collagenase only moderately. A slight inactivation of thrombin was detected.
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