A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins

Michael J Leibowitz; R. L. Soffer

A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins

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

Abstract

A soluble enzyme which catalyzes the transfer of leucine and phenylalanine from tRNA to protein has been partially purified from Escherichia coli. No activity is observed with other amino acyl tRNAs. The transfer reaction does not require magnesium ions but does require a monovalent cation and an acceptor protein such as bovine serum albumin.

Original language	English (US)
Pages (from-to)	47-53
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	36
Issue number	1
State	Published - Jul 7 1969
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry

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title = "A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins",

abstract = "A soluble enzyme which catalyzes the transfer of leucine and phenylalanine from tRNA to protein has been partially purified from Escherichia coli. No activity is observed with other amino acyl tRNAs. The transfer reaction does not require magnesium ions but does require a monovalent cation and an acceptor protein such as bovine serum albumin.",

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AB - A soluble enzyme which catalyzes the transfer of leucine and phenylalanine from tRNA to protein has been partially purified from Escherichia coli. No activity is observed with other amino acyl tRNAs. The transfer reaction does not require magnesium ions but does require a monovalent cation and an acceptor protein such as bovine serum albumin.

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