Nippon Shokakibyo Gakkai Zasshi
Online ISSN : 1349-7693
Print ISSN : 0446-6586
PURIFICATION OF HUMAN MICROSOMAL EPOXIDE HYDROLASE AND STUDY ON ITS LOCALIZATION IN HEPATOCELLULAR CARCINOMA TISSUE
Ken-ichi NODATakaro ESAKIMakoto MURATAMasaaki OGINOYuji KADOTomomi KONISHIKiwamu OKITATadayoshi TAKEMOTO
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1984 Volume 81 Issue 3 Pages 874-879

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Abstract

Human liver microsomal epoxide hydroloase (EH), which was a single polypeptide band with 50, 000 molecular weight and 361 unit/mg protein enzyme activity, was purified from an autopsied normal liver tissue by means of Lus' method. It was immunized with a rabbit to get a specific anti-human EH serum.
The localization of EH, γ-glutamyl transpeptidase (γ-GTP) and α-fetoprotien (AFP) were simultaneously studied on the tissue sections with primary hepatocellular carcinoma by the immunoand /or histochemical staining method. The intensity of EH in tumor tissues increased in 4 cases (16%), showed the equal level in 12 cases (48%) and decreased in 9 cases (36%), as compared with the surrounding non-tumor tissues. The intensity of γ-GTP or AFP in tumor tissue increased in 12 cases (48%), 19 cases (76%) respectively. There was no definite relation among their intensities in tumor tissues.
These results suggest that EH is an important protein to identify a precancerous lesion of human hepatocellular carcinoma.

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© The Japanese Society of Gastroenterology
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