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Hiroshima Journal of Medical Sciences Volume 33 Issue 4
published_at 1984-12
Purification of Thiol Protease Inhibitor from Human Lung Cancer Tissue
ヒト肺癌組織からのチオールプロテアーゼインヒビターの精製
Okumichi Tsuneo
Nishiki Masayuki
Takasugi Sumiyoshi
Yamane Motoi
Ezaki Haruo
Abstract
It was confirmed that the thiol protease inhibitory activities in human lung cancer extracts were significantly higher than normal lung tissue extracts.
Furthermore the thiol protease inhibitor was extracted from human lung cancer tissue and purified by papain-Sepharose and Sephadex G-100 column chromatographies. The purified inhibitor inhibited papain and ficin, and its molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was about 13,000.
Furthermore the thiol protease inhibitor was extracted from human lung cancer tissue and purified by papain-Sepharose and Sephadex G-100 column chromatographies. The purified inhibitor inhibited papain and ficin, and its molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was about 13,000.
About This Article
Descriptions
This research was funded in part by Grant-in-Aid for Scientific Research, Project 56480213, of the Japanese Ministry of Education.
Keywords
Thiol protease inhibitor
Human lung cancer
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