Premium
Inhibitory Activity of a Low‐molecular‐weight Proteinase Inhibitor (2,200 Mr.) against Various Proteinases
Author(s) -
Nagase Sanae,
Kawamura Mari,
Higuchi Dousei,
Takiuchi Iwao
Publication year - 1987
Publication title -
the journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.9
H-Index - 65
eISSN - 1346-8138
pISSN - 0385-2407
DOI - 10.1111/j.1346-8138.1987.tb03599.x
Subject(s) - papain , plasmin , trypsin , chemistry , cysteine proteinase inhibitors , biochemistry , sodium dodecyl sulfate , microbiology and biotechnology , kunitz sti protease inhibitor , molecular mass , macroglobulin , gel electrophoresis , polyacrylamide gel electrophoresis , collagenase , proteases , enzyme , biology , apoptosis , programmed cell death , caspase
A 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 a 2 macroglobulin (α 2 ‐M) by a double immunodiffusion test using anti‐α 2 ‐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.