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来自人肝癌细胞的膜结合芳基酰胺酶,其电泳迁移率与胎盘膜结合芳基酰胺酶相同。

Membrane-bound arylamidase from human hepatoma cells having the same electrophoretic mobility as placental membrane-bound arylamidase.

作者信息

Hiwada K, Terao M, Ono M, Kokubu T

出版信息

Clin Chim Acta. 1978 Feb 1;83(1-2):185-8. doi: 10.1016/0009-8981(78)90224-3.

Abstract

A membrane-bound arylamidase from well-differentiated hepatocellular carcinoma having the same electrophoretic mobility as placental membrane-bound arylamidase was found. The enzyme was found to be a sialoprotein and was activated by Co2+. Hepatoma membrane-bound arylamidase had a similar molecular weight (240 000) and kinetic properties to normal liver membrane-bound arylamidase, but differed from the liver enzyme with respect to electrophoretic mobility, heat stability and urea inactivation.

摘要

发现一种来自高分化肝细胞癌的膜结合芳基酰胺酶,其电泳迁移率与胎盘膜结合芳基酰胺酶相同。该酶为唾液酸蛋白,被Co2+激活。肝癌膜结合芳基酰胺酶的分子量(240 000)和动力学特性与正常肝膜结合芳基酰胺酶相似,但在电泳迁移率、热稳定性和尿素失活方面与肝酶不同。

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Comparison of human membrane-bound neutral arylamidases from small intestine, lung, kidney, liver and placenta.
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