Abstract
Abstract A large sample of highly purified phenylalanine transfer ribonucleic acid from Escherichia coli B was prepared by reversed phase chromatography followed by gel filtration to remove ribonucleic acid contaminants of higher molecular weight. The phenylalanine acceptance and terminal adenosine content of this sample were identical, indicating that the sample was all active phenylalanine transfer ribonucleic acid. An independent measurement of purity obtained on a weight basis gave a minimum value of 83%. Preliminary data indicate that the phenylalanine transfer ribonucleic acid molecular weight is approximately 26,000.
Highlights
A large sample of highly purified phenylalanine transfer ribonucleic acid from Escherichia coli B was prepared by reversed phase chromatography followed by gel filtration to remove ribonucleic acid contaminants of higher molecular weight
An independent measurement of purity obtained on a weight basis gave a minimum value of 83 %
This paper describes the preparation of a sample of highly purified tRNAPhe from Escherichia coli B
Summary
This crude enzyme was used in the amino acid acceptance assay of the many chromatographic fractions and in assaying the tRNAPhe. A sample of highly purified E. coli B phenylalanyl-tRNA synthetase was kindly supplied by Dr M.
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