タイトル無し

概要

論文の詳細を見る
The alkaline phosphatase (AP) isoenzyme from colonic carcinoma of the highly inbred Wistar-Furth (W-F) strain rat (carcinoma AP) was compared with AP from colonic mucosa of the same strain rat without colonic carcinoma (non-carcinoma AP), and also AP from normal rat colon of Wistar strain (normal AP) from which WF strain is derived.The sepcific activity of carcinoma AP was ten-fold higher than that of normal AP, whereas that of non-carcinoma AP was almost the same as that of normal AP.On polyacrylamide gel electrophoresis, carcinoma AP migrated as a slow-moving band, which was retarded by the treatment with neuraminidase.Non-carcinoma AP and normal AP electrophoresed in three bands and two bands, respectively. Their electrophoretic mobilities were not affected by the treatment with neuraminidase. No significant differences between non-carcinoma AP and normal AP were found in other enzymatic properties. However, carcinoma AP was found to be completely different from APs of the other two sources.
財団法人日本消化器病学会の論文