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Isolation and binding properties of leucyl-tRNA synthetase from Escherichia coli MRE 600

โœ Scribed by Stefica Granda; Helmut Hustedt; Josef Flossdorf; Maria-Regina Kula

Publisher
Springer
Year
1979
Tongue
English
Weight
513 KB
Volume
24
Category
Article
ISSN
0300-8177

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โœฆ Synopsis

A procedure for the large-scale isolation of leucyl-tRNA synthetase from E. cole MRE 600 is described: The enzyme was purified about 320-fold to homogeneity by precipitation with cetyl-trimethyl-ammonium bromide, two consecutive chromatographies on DEAE-cellulose and three on hydroxyapatite with an over-all yield of 4%. The molecular weight of leucyl-tRNA synthetase from E. coli MRE 600 was found to be 99 000 daltons. Bindings studies by ultracentrifugation and equilibrium partition showed that the enzyme binds leucine, leucyl-adenylate and tRNA Leu, each in a 1 : 1 stoichiometry. For ATP only a very weak binding to the enzyme could be observed, which did not allow the evaluation of the complex stoichiometry. The presence of ATP was not required for the binding of leucine or tRNA to leucyl-tRNA synthetase from E. coli MRE 600.

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โœ Binding, Ron ;Romansky, Gary ;Bitner, Rex ;Kuempel, Peter ๐Ÿ“‚ Article ๐Ÿ“… 1981 ๐Ÿ› Springer ๐ŸŒ English โš– 805 KB

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