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Isolation and some properties of a 34‐kDa‐membrane protein that may be responsible for ribosome binding in rat liver rough microsomes
Author(s) -
Ichimura Tohru,
Ohsumi Tomoya,
Shindo Yukiko,
Ohwada Tamotsu,
Yagame Harutaka,
Mornose Yasunori,
Omata Saburo,
Sugano Hiroshi
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80391-s
Subject(s) - ribosome , microsome , organelle , biochemistry , membrane , liposome , chemistry , binding protein , membrane protein , biology , rna , enzyme , gene
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.