Kinetic parameters of tryptophan: tRNA ligase catalyzed ATP-(32P) pyrophosphate exchange as an approach to extimation of the order of substrate binding. [electronic resource]

By:

Favorova, O O

Contributor(s):

Kochkina, L L
Meldrajs, J A
Kisselev, L L
Zinoviev, V V

Producer: 19751126Description: 322-6 p. digitalISSN:

0014-5793

Subject(s):

Adenosine Triphosphate -- metabolism
Amino Acyl-tRNA Synthetases -- metabolism
Animals
Binding Sites
Cattle
Diphosphates -- metabolism
Kinetics
Protein Binding
Tryptamines -- metabolism
Tryptophan -- analogs & derivatives
Tryptophan-tRNA Ligase -- metabolism

Online resources:

Available from publisher's website

In: FEBS letters vol. 56

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Kinetic parameters of tryptophan: tRNA ligase catalyzed ATP-(32P) pyrophosphate exchange as an approach to extimation of the order of substrate binding.

APA

Favorova O. O., Kochkina L. L., Meldrajs J. A., Kisselev L. L. & Zinoviev V. V. (19751126). Kinetic parameters of tryptophan: tRNA ligase catalyzed ATP-(32P) pyrophosphate exchange as an approach to extimation of the order of substrate binding. : FEBS letters.

Chicago

Favorova O O, Kochkina L L, Meldrajs J A, Kisselev L L and Zinoviev V V. 19751126. Kinetic parameters of tryptophan: tRNA ligase catalyzed ATP-(32P) pyrophosphate exchange as an approach to extimation of the order of substrate binding. : FEBS letters.

Harvard

Favorova O. O., Kochkina L. L., Meldrajs J. A., Kisselev L. L. and Zinoviev V. V. (19751126). Kinetic parameters of tryptophan: tRNA ligase catalyzed ATP-(32P) pyrophosphate exchange as an approach to extimation of the order of substrate binding. : FEBS letters.

MLA

Favorova O O, Kochkina L L, Meldrajs J A, Kisselev L L and Zinoviev V V. Kinetic parameters of tryptophan: tRNA ligase catalyzed ATP-(32P) pyrophosphate exchange as an approach to extimation of the order of substrate binding. : FEBS letters. 19751126.

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