Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Biochim Biophys Acta October 15, 1975; 407 (3): 325-37.

Biogenesis of plasmalemmal glycoproteins. Intracellular site of synthesis of mouse liver plasmalemmal 5''-nucleotidase as determined by the sub-cellular location of messenger RNA coding for 5''-nucleotidase.

Bergeron JJ , Berridge MV , Evans WH .

1. Free and membrane-bound mouse liver polyribosomes were separated by prolonged density-gradient centrifugation of the post-mitochondrial supernatant. RNA was extracted from free and membrane-bound polyribosomes and mRNA purified by oligo(dT)-cellulose column chromatography. 2. Antisera against purified mouse liver plasma membrane 5''-nucleotidase and moust albumin were prepared and characterized. 3. Microinjection of equivalent amounts of mRNA from free and membrane-bound liver polyribosomes into Xenopus laevis oocytes indicated by immuno precipitation and sodium dodecylsulphate gel electrophoresis a higher proportion of mRNA coding for 5''-nucleotidase and serum albumin in membrane-bound polyribosomes than free polyribosomes. 4. Although small, significant amounts of serum albumin and 5''-nucleotidase were also coded for by mRNA purified from free polyribosomes. The results suggest that in vivo, mRNA in mouse liver membrane-bound polyribosomes codes for the synthesis of 17 times more 5''-nucleotidase than does the mRNA in free polyribosomes.

PubMed ID: 810623
Article link: Biochim Biophys Acta