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Electrophoretic characterization of heat‐stable squamous cell carcinoma antigen
Author(s) -
Nawata Shugo,
Suminami Yoshinori,
Hirakawa Hiroshi,
Murakami Akihiro,
Umayahara Kenji,
Ogata Hidenobu,
Numa Fumitaka,
Nakamura Kazuyuki,
Kato Hiroshi
Publication year - 2001
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200109)22:16<3522::aid-elps3522>3.0.co;2-#
Subject(s) - basal cell , characterization (materials science) , electrophoresis , antigen , chemistry , materials science , chromatography , nanotechnology , pathology , biology , immunology , medicine
The aim of this study was to investigate the heat stability of squamous cell carcinoma (SCC) antigen, a tumor‐associated serine proteinase inhibitor (serpin), in tumor tissue extract by electrophoretic methods. After heat treatment at 70°C for 2 h, the tumor tissue extract showed a single main protein band of 45 kDa on sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) which reacted with a monoclonal antibody specific for SCC antigen. The heat‐stable SCC antigen was separated by two‐dimensional electrophoresis (2‐DE) into four spots with p I 6.4–5.9 and M r 44 500–45 000 of SCC antigen‐1. Furthermore, the SCC antigen‐1 still showed its inhibitory activity against a cysteine proteinase, papain, by gelatin zymography. These results suggest that heat treatment of protein sample at 70°C for 2 h may be a useful method for a partial purification of SCC antigen‐1 which can inhibit lysosomal cysteine proteinases such as cathepsin L, S, and K.