Studies on rat liver catalase. XI. Site of synthesis and segregation by stripped ER membranes.:XI. Site of Synthesis and Segregation by Stripped ER Membranes
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- TOBE Takashi
- Department of Biochemistry, School of Pharmaceutical Sciences, Showa University
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- HIGASHI Tokuhiko
- Department of Biochemistry, School of Pharmaceutical Sciences, Showa University
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説明
We reinvestigated the site of synthesis of rat liver catalase, and it has been reconfirmed that catalase is synthesized not only by free polysomes but also by membrane-bound polysomes. Considerable amounts of nascent catalase on rough microsomes were released from the membrane into the medium upon incubation with puromycin, not transported directly into the intracisternal cavity of microsomes. On the other hand, catalase newly synthesized in vitro was shown to be segregated by stripped rat liver microsomal membranes in a state resistant to proteolysis. Since this segregation occurred without coupled protein synthesis, catalase appears to be transported by a mechanism different from co-translational transfer. A hypothesis is presented regarding the mechanism of intracellular transport of liver catalase.
収録刊行物
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- The Journal of Biochemistry
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The Journal of Biochemistry 88 (5), 1341-1347, 1980
The Japanese Biochemical Society
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詳細情報 詳細情報について
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- CRID
- 1571698603040776064
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- NII論文ID
- 130003541528
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- ISSN
- 0021924X
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles