Isolation and some properties of a 34‐kDa‐membrane protein that may be responsible for ribosome binding in rat liver rough microsomes

FEBS Letters

Ichimura, Tohru³  Omata, Saburo¹  Sugano, Hiroshi¹  Ohsumi, Tomoya³  Shindo, Yukiko¹  Yagame, Harutaka¹  Ohwada, Tamotsu¹  Mornose, Yasunori² 

[1] Department of Biochemistry, Faculty of Science, Niigata University, 2-Igarashi, Niigata 950-21, Japan;Second Research Laboratories, Kissei Pharmaceutical Co., Nagano 399-83, Japan;Department of Biosystem Science, Graduate School of Science and Technology, Faculty of Science, Niigata University, 2-Igarashi, Niigata 950-21, Japan

关键词: Ribosome-binding protein;    Ribosome;    Rough microsome;    Purification: Liposome;    RM;    rough microsomes;    SM;    smooth microsomes;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(92)80391-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have isolated, by hydroxyapatite chromatography with a non ionic detergent and a high salt concentration, a non-glycosylated, membrane protein with a relative molecular weight of 34 kDa that had previously been found to be a major constituent of the membrane protein fraction showing ribosoine-binding activity derived from rat liver rough microsomes (RM). The isolated 34 kDa protein (p34), when incorporated into a liposome model membrane, exhibited significant binding activity toward ribosomes, its binding properties being similar to those observed with intact R.M. immunochemical analyses using antibodies directed against p34 suggested that it is a membrane-embedded RM surface protein, which is specifically localized in ribosome-attached organelles and widely distributed among mammalian tissues. These results would constitute evidence that p34 is a likely candidate for an RM ribosome-binding, protein.

【 授权许可】

Unknown