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30‐kDa Trypsin‐like Proteases in the Plantar Stratum Corneum
Author(s) -
ChangYi Cui,
Takahashi Masae,
Tezuka Tadashi
Publication year - 1997
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.1346-8138.1997.tb02830.x
Subject(s) - proteases , trypsin , stratum corneum , biochemistry , leupeptin , protease , kunitz sti protease inhibitor , chemistry , aprotinin , zymography , serine , enzyme , serine protease , chymotrypsin , casein , biology , medicine , genetics , surgery
The casein digestible proteases in human plantar stratum corneum were determined to be about 75‐kDa, 30‐kDa and 25‐kDa in molecular weight by zymography. The enzymatic activity of the 75‐kDa and 25‐kDa proteases was specifically inhibited by chymostatin, which is an inhibitor of chymotrypsin‐like serine proteases, and the proteases around 30‐kDa were inhibited by leupeptin, a trypsin‐like serine protease inhibitor. The enzymatic activity of all these proteases was inhibited by aprotinin. The 30‐kDa trypsin‐like proteases were heat‐stable; their enzymatic activity still remained even after heating at 100°C for 60 minutes. Their optimal pH was around 9, and the activity was higher in the outer part of the stratum corneum than in the inner part.