Catalytic activation of transfer ribonucleic acid by a mammalian protein.
A tRNA activator has been isolated from mammalian organs which increases the capability of tRNA to accept certain amino acids through the action of mammalian aminoacyl-tRNA synthetases. This activity may be separated from the aminoacyl-tRNA synthetases for isoleucine, lysine, serine, and methionine by fractionation of liver or pancreas cytosol with ammonium sulfate or by chromatography over Sephadex G-200. The tRNA activating material is nondialyzable and is destroyed by trypsin or short heating. It acts catalytically. A molecular weight of approximately 45,000 was obtained by chromatography of tRNA activator on a calibrated Sephadex G-150 column. Activator increases acceptance of yeast tRNA for the amino acids isoleucine, leucine, lysine, serine, and methionine. It shows higher activity on liver tRNAMet f, tRNAMet m, and tRNALys than on unfractionated liver tRNA. Removal of protein from mammalian tRNA by extra phenol extractions, chromatography, or proteinase treatment increases its response to activator.[1]References
- Catalytic activation of transfer ribonucleic acid by a mammalian protein. Dickman, S.R., Boll, D.J. Biochemistry (1976) [Pubmed]
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