Purification and characterization of the major 50‐kDa repressor protein from cytoplasmic mRNP of rabbit reticulocytes
Open Access
- 3 March 1993
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 212 (3) , 633-638
- https://doi.org/10.1111/j.1432-1033.1993.tb17701.x
Abstract
A 50-kDa protein has been purified to homogeneity from free mRNP of rabbit reticulocytes. This protein, designated as p50, is present within both free mRNP (approximately 4 mol protein/mol globin mRNA) and polyribosomal mRNP (approximately 2 mol protein/mol globin mRNA). p50 is a basic protein (pI ∼ 9.5) and is characterized by a high glycine content of approximately 20%. Nitrocellulose-filter analysis has shown that p50 interacts with globin mRNA with an association constant of approximately 2.5 × 108 M−1 (100 mM KAc, 4°C). Various RNA and polyribonucleotides have the following relative affinity for p50; poly(G) > poly(U) > globin mRNA ∼ 16S rRNA > poly(A) > poly(C). p50 can be phosphorylated both in vitro and in vivo.Keywords
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