Abstract

“Renaturable” leucine transfer ribonucleic acid from baker’s yeast was found by Lindahl et al. [l] to be able to exist in a relatively stable denatured configuration which has only low amino acid acceptor activity. Incubation at 60’ for 5 min, followed by slow cooling in the presence of magnesium ion, was found to disrupt the incorrect cornformation and allow renaturation to -the native, biologically active structure. Although the physiological significance of the reversible denaturation process, if any, is not known, it is of interest to try to determine if there is a unique feature of the primary or secondary structure that would account for the stability of the second, inactive conformation. The “renaturable leucine tRNA (tRNAy)** was purified in our laboratory by sucessive chromatography on benzoylated DEAE cellulose and Sephadex G-100 columns [2]. We determined the nucleotide sequence of this tRNA [3] by Holley’s method [4]. In this paper, we would like to report our results and compare them with those recently reported by Kowalski et al. [S] . Purified tRNALeU was digested with pancreatic ribonuclease [2] .“The identity of the products from this digestion are shown in table 1. Sequence analyses

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