Affinity Labelling of tRNA Nucleotidyltransferase from Baker's Yeast with tRNAPhe Modified on the 3′‐Terminus
Open Access
- 1 August 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 67 (1) , 215-221
- https://doi.org/10.1111/j.1432-1033.1976.tb10652.x
Abstract
2′‐Deoxy‐2′‐amino‐cytidylic acid can be incorporated into position 75 of tRNAPhe from yeast by tRNA nucleotidyltransferase yielding tRNAPhe‐C‐C(2′NH2). tRNAPhe‐C‐C(2′NH2) can be reacted with the N‐hydroxysuccinimide esters of bromoacetic acid and of mercuriacetic acid to yield the derivatives tRNAPhe‐C‐C(2′NHCOCH2Br) and tRNAPhe‐C‐C(2′NHCOCH2Hg+OH‐). Each of these reactive tRNAs inactivates tRNA nucleotidyltransferase from yeast with similar kinetics. The enzyme can be protected against inhibition by its substrates tRNAPhe‐C and tRNAPhe ‐C‐C as well as ATP and CTP. A covalent. isolatable 1:1 complex between tRNAPhe ‐C‐C(2′NHCOCH2Br) and the enzyme was formed, but could not be found when the enzyme had previously been inactivated with p‐hydroxymerecuribenzoate.This publication has 27 references indexed in Scilit:
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