CU,ZN SUPEROXIDE-DISMUTASE IS A PEROXISOMAL ENZYME IN HUMAN FIBROBLASTS AND HEPATOMA-CELLS

被引：195

作者：

KELLER, GA ^{[1
]}

WARNER, TG ^{[1
]}

STEIMER, KS ^{[1
]}

HALLEWELL, RA ^{[1
]}

机构：

[1] CHIRON CORP,EMERYVILLE,CA 94608

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 16期

关键词：

D O I：

10.1073/pnas.88.16.7381

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The intracellular localization of Cu,Zn superoxide dismutase (superoxide:superoxide oxidoreductase, EC 1.15.1.1) has been examined by immunofluorescence using four monoclonal anti-Cu,Zn superoxide dismutase antibodies raised against a recombinant human Cu,Zn superoxide dismutase derivative produced and purified from Escherichia coli. Colocalization with catalase, a peroxisomal matrix enzyme, was used to demonstrate the peroxisomal localization of Cu,Zn superoxide dismutase in human fibroblasts and hepatoma cells. In the fibroblasts of Zellweger syndrome patients, the enzyme is not transported to the peroxisomal ghosts but, like catalase, remains in the cytoplasm. In addition, immunocryoelectron microscopy of yeast cells expressing human Cu,Zn superoxide dismutase showed that the enzyme is translocated to the peroxisomes.

引用

页码：7381 / 7385

页数：5

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