title: The binding of monoribosomes, oligoribosomes and polyribosomes to reticular membranes from rat liver.
abstract: 1. The activity of the enzyme protein disulphide-isomerase (EC 5.3.4.1) was used to measure the binding of ribosomal fractions to reticular membranes from the liver of unstarved male rats. 2. Membranes degranulated by treatment with KCl plus puromycin and washed by centrifugation through 0.5 M-KCl bound oligoribosomes but not monoribosomes. 3. Substitution of 0.25 M-KCl for 0.5 M-KCl in the wash solution produced membranes that bound monoribosomes and 60 S subunits in addition to oligoribosomes. 4. The binding of all classes of ribosomes to smooth and 'lightly granulated' rough membranes was activated by oestradiol. The hormone activation was much greater with polyribosomes from fed rats than for monoribosomes or oligoribosomes from starved rats. 5. Exposure of rough membranes to centrifugal forces caused them to undergo partial degranulation, as demonstrated by unmasking of protein disulphide-isomerase activity.
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D004220:Disulfides; D004958:Estradiol / Q000494:pharmacology; D007535:Isomerases / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D008297:Male; D011132:Polyribosomes / Q000378:metabolism*; D011506:Proteins; D051381:Rats; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*
chemical_list: D004220:Disulfides; D011506:Proteins; D004958:Estradiol; D007535:Isomerases