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Protein synthesis in rabbit reticulocytes. XIII. Lack of mRNA (poly r (A)) binding activity in highly purified EIF-1.
Authors:A Majumdar  S Reynolds  N K Gupta
Affiliation:Department of Chemistry University of Nebraska-Lincoln Lincoln, Nebraska 68588 USA
Abstract:Met-tRNAfMet binding factor (EIF-1) has been purified more than 100 fold over crude high salt (0.5 M KCl) ribosomal wash. The purified factor binds 2 nmoles Met-tRNAfMet per mg protein and shows very little poly r(A) binding activity. Crude ribosomal high salt wash possesses significant amounts of poly r(A) binding activity and also binds to other RNAs. The bulk of this unspecific RNA binding protein is separated from EIF-1 by DEAE-cellulose chromatography.
Keywords:EIF-1  eukaryotic initiation factor 1
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