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2016•Unpublished venueRequires access

Characterization of Messenger Ribonucleo

Ajit Kumar, Uno Lindberg

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Abstract

Messenger ribonucleoprotein and mRNA from KB-cells were isolated under conditions designed to minimize nonspecific RNA-protein interaction and to minimize degradation by contaminating ribonucleases. A large fraction, 60-70%, of the messenger ribonucleo- protein from polysomes dissociated in vitro by either EDTA or puromycin sedimented faster than the large ribo- some subunit. Messenger ribonucleoprotein particles with sedimentation coefficients up to 200 S were observed. Released mRNA was also large, with maximal molecular weights around 5 X 106.

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What this paper is about

Messenger ribonucleoprotein and mRNA from KB-cells were isolated under conditions designed to minimize nonspecific RNA-protein interaction and to minimize degradation by contaminating ribonucleases. A large fraction, 60-70%, of the messenger ribonucleo- protein from polysomes dissociated in vitro by either EDTA or puromycin sedimented faster than the large ribo- some subunit. Messenger ribonucleoprotein particles with sedimentation coefficients up to 200 S were observed. Released mRNA was also large, with maximal molecular weights around 5 X 106.

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Available abstract

Messenger ribonucleoprotein and mRNA from KB-cells were isolated under conditions designed to minimize nonspecific RNA-protein interaction and to minimize degradation by contaminating ribonucleases. A large fraction, 60-70%, of the messenger ribonucleo- protein from polysomes dissociated in vitro by either EDTA or puromycin sedimented faster than the large ribo- some subunit. Messenger ribonucleoprotein particles with sedimentation coefficients up to 200 S were observed. Released mRNA was also large, with maximal molecular weights around 5 X 106.

Key concepts: Messenger RNP, Polysome, Messenger RNA, Ribonucleoprotein, Puromycin, Ribosome, Chemistry, Protein subunit

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