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Clinical Chemistry 23: 1615-1623, 1977;
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Clinical Chemistry, Vol 23, 1615-1623, Copyright © 1977 by American Association for Clinical Chemistry

A fetal intestinal-type alkaline phosphatase in hepatocellular carcinoma tissue

K Higashino, R Otani, S Kudo and Y Yamamura

We examined 19 hepatoma tissues for alkaline phosphatase isoenzyme and found that six have both the Kasahara isoenzyme and an alkaline phosphatase with a unique electrophoretic mobility, in addition to the liver-type enzyme. From two of six carcinoma tissues, the abnormal enzyme was partly purified and subjected to a detailed analysis, which clarified that the abnormal enzyme resembled a fetal intestinal alkaline phosphatase in most of its enzymic and immunologic properties and also in properties that reflect enzyme structure. This fetal intestinal-type alkaline phosphatase was not found in 24 specimens of normal liver from adults. The relevance of fetal intestinal-type alkaline phosphatase to Kasahara isoenzyme and adult intestinal alkaline phosphatase is discussed. The fetal and adult intestinal alkaline phosphatases differ in electrophoretic mobility, heat stability, and reactivity with concanavalin A. The adult-type enzyme has two components; only the electrophoretically slower, neuraminidase- resistant one is described here.


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M.-H. Le Du and J. L. Millan
Structural Evidence of Functional Divergence in Human Alkaline Phosphatases
J. Biol. Chem., December 13, 2002; 277(51): 49808 - 49814.
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Copyright © 1977 by the American Association for Clinical Chemistry.