RNA-Binding Proteins of Rabbit Reticulocytes. Isolation and Electrophoretic Characteristics
- 1 October 1978
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 90 (3) , 517-525
- https://doi.org/10.1111/j.1432-1033.1978.tb12631.x
Abstract
A complete set of RNA-binding proteins was isolated from the ribosome-free extract of rabbit reticulocytes using the method of affinity chromatography on RNA covalently coupled with Sepharose. The purity of the isolated proteins was no less than 90%. These proteins comprised about 1% of the total protein of the extract and included the main polypeptide chains of 3 sizes, with MW of about 95,000, 49,000 and 36,000, as well as numerous minor components. An analogous set of proteins was observed as a result of chromatography of the extract on a column of poly(U) covalently coupled with Sepharose. The protein with the 49,000 MW had the highest affinity for RNA.This publication has 20 references indexed in Scilit:
- Rat liver soluble nuclear and cytoplasmic proteins with high affinity to polynucleotidesFEBS Letters, 1975
- Mammalian proteins with affinity to polynucleotides: Isolation by affinity chromatography from rat liver cytosol and nucleosolFEBS Letters, 1974
- RNA‐binding protein from rabbit reticulocyte extractFEBS Letters, 1974
- Isolation of proteins with high affinity for dRNAFEBS Letters, 1974
- RNA‐binding protein factor of animal cell extractsFEBS Letters, 1971
- Preparation of sepharose-bound poly (rI:rC)Biochemical and Biophysical Research Communications, 1971
- Messenger RNA in rat liver polyribosomes: Evidence that it exists as ribonucleoprotein particlesJournal of Molecular Biology, 1968
- Messenger RNA-protein complexes and newly synthesized ribosomal subunits: Analysis of free particles and components of polyribosomesJournal of Molecular Biology, 1968
- Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gelsBiochemical and Biophysical Research Communications, 1967
- Nuclear Ribonucleoprotein Particles Containing Messenger Ribonucleic AcidNature, 1966