The effect of an intramolecular cross-link on reversible denaturation in tryptophan transfer ribonucleic acid from Escherichia coli.
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Biomedical subjects
Publications and source records attributed to R H Buckingham.
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1. Two minor protein fractions (B and C) were separated from histone F1 by chromatography on DEAE-cellulose. Fraction B was acidic. 2. Uptake of (32)P in vivo into histone F1 but not into fractions B and C was stimulated by partial hepatectomy. 3. It is suggested that partial hepatectomy causes an increase in the number of histone F1 molecules phosphorylated.
Four subfractions of histone F1 from rat thymus were obtained by preparative polyacrylamide-gel electrophoresis. These subfractions are closely related in primary structure but show marked differences in radioactivity when derived from rat thymus nuclei labelled in vitro with [(32)P]phosphate.
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Using different ribonucleases we have studied the digestion pattern of the two methionine accepting tRNAs, the initiator tRNAfMet and the elongator tRNAmMet from E. coli. The positions and intensities of cleavages are compared to those obtained when the tRNAs are complexed to methionyl-tRNA synthetase. Our results, in comparison with other studies, suggest a general pattern of interaction between tRNAs and their cognate synthetases including the amino acid stem and the anticodon region. Furthermore a lack of involvement of the central region and especially the extra arm seems to be a unique feature of the initiator tRNAMetf.