Utilization of selenocysteine by a cysteinyl-tRNA synthetase from Phaseolus aureus [Mung beans]

An L-cysteinyl-tRNA synthetase (EC 6.1.1.16) from Phaseolus aureus has been purified approximately 200-fold. The enzyme uses seleno-cysteine 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...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1976-09, Vol.58 (3), p.248-252
Main Authors: Shrift, A, Bechard, D, Harcup, C
Format: Article
Language:English
Subjects:
Amino acids
Chromatography
Electrophoresis
Enzymes
Gels
Molecular weight
Phosphates
Selenium
Sodium
Transfer RNA
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Description
Summary:An L-cysteinyl-tRNA synthetase (EC 6.1.1.16) from Phaseolus aureus has been purified approximately 200-fold. The enzyme uses seleno-cysteine 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.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.58.3.248