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. 1976 Sep;58(3):248–252. doi: 10.1104/pp.58.3.248

Utilization of Selenocysteine by a Cysteinyl-tRNA Synthetase from Phaseolus aureus1

Alex Shrift a, Daniel Bechard a,2, Craig Harcup a,3, Leslie Fowden b
PMCID: PMC542225  PMID: 16659657

Abstract

An l-cysteinyl-tRNA synthetase (EC 6.1.1.16) from Phaseolus aureus has been purified approximately 200-fold. The enzyme uses selenocysteine as substrate in the ATP-PPi exchange assay; other cysteine analogs were inactive. The molecular weight as determined by Sephadex G-200 column chromatography is about 61,000; sodium dodecyl sulfate and 8 m urea acrylamide gel electrophoresis indicate that the enzyme is a dimer consisting of two identical monomers of molecular weight 30,000. A method for the preparation of selenocysteine from selenocystine is described.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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