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Serine protease inhibitor activity of recombinant squamous cell carcinoma antigen towards chymotrypsin, as demonstrated by sodium dodecyl sulfatepolyacrylamide gel electrophoresis
Author(s) -
Nawata Shugo,
Tsunaga Nagato,
Numa Fumitaka,
Tanaka Tatehiko,
Nakamura Kazuyuki,
Kato Hiroshi
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.11501601173
Subject(s) - serpin , sodium dodecyl sulfate , chymotrypsin , trypsin , serine protease , gel electrophoresis , microbiology and biotechnology , proteases , chemistry , biochemistry , serine proteinase inhibitors , serine , ovalbumin , antigen , protease , polyacrylamide gel electrophoresis , recombinant dna , enzyme , biology , immunology , gene
Squamous cell carcinoma (SCC) antigen was tested, by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, for its ability to inhibit the activity of serine proteases, i.e. , trypsin, chymotrypsin and elastase. We demonstrated that the serine protease inhibitor (serpin) of SCC antigen is specific for chymotrypsin. Preincubation of chymotrypsin with recombinant SCC antigen inhibited chymotryptic digestion of gelatin and ovalbumin through the formation of sodium dodecyl sulfate‐stable complexes. These findings promote understanding of the biological functions of SCC antigen as serpin in the stratification of the normal squamous cells and in the malignant behaviour of the tumor cells.