An arginyl-transfer ribonucleic Acid protein transferase from cereal embryos.

Abstract:

:Embryos from rice (Oryza sativa L. var. Bluebonnet) and wheat (Triticum aestivum L.) contain an aminoacyl-tRNA protein transferase which transfers arginine from arginyl-tRNA to the N terminus of a protein acceptor. The activity was measured in vitro in a reaction mixture containing embryo supernatant fraction, buffer, sulfhydryl reagent, and arginyl-tRNA. It was not dependent on the usual cofactors for ribosomal protein synthesis, nor was it sensitive to cycloheximide or puromycin. However, the activity was inhibited by ribonuclease. The enzyme was purified 33-fold from a crude homogenate of rice embryos. An apparent endogenous substrate from rice embryos was prepared free of transferase activity; however, the transferase was not purified sufficiently to show absolute dependence on the presence of this endogenous substrate.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Manahan CO,App AA

doi

10.1104/pp.52.1.13

subject

Has Abstract

pub_date

1973-07-01 00:00:00

pages

13-6

issue

1

eissn

0032-0889

issn

1532-2548

journal_volume

52

pub_type

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