Isolation and chromatographic behaviour of phenylalanine tRNA from barley embryos |
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Authors: | D. Labuda Z. Janowicz T. Haertle J. Augustyniak |
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Affiliation: | Institute of Biochemistry of Poznań Universities, 61701 Poznań, ul. Fredry 10, Poland |
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Abstract: | Two fractions of phenylalanine tRNA (tRNAPhe1 and tRNAPhe2) were purified by BD-cellulose and RPC-5 chromatography of crude tRNA isolated from barley embryos. Successive RPC-5 rechromatography runs of tRNAPhe2 showed its conversion into more stable tRNAPhe1, suggesting that the two fractions have essentially the same primary structure. Both tRNAPhe1 and tRNAPhe2 had about the same acceptor activity, but tRNAPhe2 was aminoacylated much faster than tRNAPhe1. RPC-5 chromatography of crude aminoacylated tRNA showed higher contents of phe-tRNAPhe2 than of phe-tRNAPhe1 but the ratio of these two fractions estimated by relative fluorescence intensity was about 1. Fluorescence spectra of tRNAPhe from barley embryos suggest that it contains Y base similar to Yw from wheat tRNAPhe. |
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