Affinity chromatography of rat liver aminoacyl-tRNA synthetase complex

Chi Van Dang; David C.H. Yang

doi:10.1016/0006-291X(78)91302-5

Affinity chromatography of rat liver aminoacyl-tRNA synthetase complex

Chi Van Dang, David C.H. Yang

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

The affinity column lysyldiaminohexyl-Sepharose 4B has been synthesized for the purification of aminoacyl-tRNA synthetase complexes. Lysyl-tRNA synthetase (EC 6.1.1.6) bound specifically to the Sepharose-bound lysine. The purified lysyl-tRNA synthetase was associated with arginyl-tRNA synthetase (EC 6.1.1.16) and sedimented at 18S and 12S. A 24S lysyl-tRNA synthetase bound specifically to the affinity column and also found associated with arginyl-tRNA synthetase. The results favor the model of a heterotypic multienzyme complex of mammalian aminoacyl-tRNA synthetases.

Original language	English (US)
Pages (from-to)	709-714
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	80
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(78)91302-5
State	Published - Feb 28 1978
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry
Cell Biology

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10.1016/0006-291X(78)91302-5

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title = "Affinity chromatography of rat liver aminoacyl-tRNA synthetase complex",

abstract = "The affinity column lysyldiaminohexyl-Sepharose 4B has been synthesized for the purification of aminoacyl-tRNA synthetase complexes. Lysyl-tRNA synthetase (EC 6.1.1.6) bound specifically to the Sepharose-bound lysine. The purified lysyl-tRNA synthetase was associated with arginyl-tRNA synthetase (EC 6.1.1.16) and sedimented at 18S and 12S. A 24S lysyl-tRNA synthetase bound specifically to the affinity column and also found associated with arginyl-tRNA synthetase. The results favor the model of a heterotypic multienzyme complex of mammalian aminoacyl-tRNA synthetases.",

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T1 - Affinity chromatography of rat liver aminoacyl-tRNA synthetase complex

AU - Dang, Chi Van

AU - Yang, David C.H.

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Y1 - 1978/2/28

N2 - The affinity column lysyldiaminohexyl-Sepharose 4B has been synthesized for the purification of aminoacyl-tRNA synthetase complexes. Lysyl-tRNA synthetase (EC 6.1.1.6) bound specifically to the Sepharose-bound lysine. The purified lysyl-tRNA synthetase was associated with arginyl-tRNA synthetase (EC 6.1.1.16) and sedimented at 18S and 12S. A 24S lysyl-tRNA synthetase bound specifically to the affinity column and also found associated with arginyl-tRNA synthetase. The results favor the model of a heterotypic multienzyme complex of mammalian aminoacyl-tRNA synthetases.

AB - The affinity column lysyldiaminohexyl-Sepharose 4B has been synthesized for the purification of aminoacyl-tRNA synthetase complexes. Lysyl-tRNA synthetase (EC 6.1.1.6) bound specifically to the Sepharose-bound lysine. The purified lysyl-tRNA synthetase was associated with arginyl-tRNA synthetase (EC 6.1.1.16) and sedimented at 18S and 12S. A 24S lysyl-tRNA synthetase bound specifically to the affinity column and also found associated with arginyl-tRNA synthetase. The results favor the model of a heterotypic multienzyme complex of mammalian aminoacyl-tRNA synthetases.

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Affinity chromatography of rat liver aminoacyl-tRNA synthetase complex

Abstract

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