title: Characterization of the rough endoplasmic reticulum ribosome-binding activity.
abstract: The rough endoplasmic reticulum membranes of mammalian cells contain specific ribosome-binding sites. A purification to apparent homogeneity of a negatively charged protein (ERp180) of relative molecular mass 180,000 (180 K) was reported which was proposed to function as a rough endoplasmic reticulum ribosome receptor. We report here that ribosome-binding site activity quantitatively solubilized from rough endoplasmic reticulum membranes does not cofractionate with ERp180. By contrast, ribosome-binding site activity fractionates as a much smaller, positively charged protein.
authors.affiliation: Department of Biochemistry and Biophysics, University of California Medical School, San Francisco 94143-0448.
authors.forename: J M
authors.initials: JM
authors.lastname: Nunnari
authors.forename: D L
authors.initials: DL
authors.lastname: Zimmerman
authors.forename: S C
authors.initials: SC
authors.lastname: Ogg
authors.forename: P
authors.initials: P
authors.lastname: Walter
mesh_terms: D000818:Animals; D001665:Binding Sites; D004285:Dogs; D004721:Endoplasmic Reticulum / Q000737:chemistry* / Q000378:metabolism; D066298:In Vitro Techniques; D007425:Intracellular Membranes / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008970:Molecular Weight; D011956:Receptors, Cell Surface / Q000737:chemistry; D012270:Ribosomes / Q000378:metabolism*
chemical_list: D008565:Membrane Proteins; D011956:Receptors, Cell Surface