The Isolation and Properties of Phenylalanyl Ribonucleic Acid Synthetase from Escherichia coli B

Phenylalanyl ribonucleic acid synthetase has been isolated from Escherichia coli and is 93% pure as determined by analytical centrifugation and gel electrophoresis. The procedure is adaptable to large scale preparation. No other aminoacyl-RNA synthetases are present in the purified preparation. The...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 242; no. 5; pp. 1060 - 1064
Main Author Stulberg, M P
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 10.03.1967
Subjects
Chromatography
Escherichia coli - enzymology
Hydroxyapatites
Ligases - analysis
Ligases - metabolism
Phenylalanine
RNA, Bacterial
RNA, Transfer - metabolism
Ultracentrifugation
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Summary:Phenylalanyl ribonucleic acid synthetase has been isolated from Escherichia coli and is 93% pure as determined by analytical centrifugation and gel electrophoresis. The procedure is adaptable to large scale preparation. No other aminoacyl-RNA synthetases are present in the purified preparation. The molecular weight of the enzyme is 181,000, with an s 20, w of 8.6. Optimal reaction conditions have been determined with highly purified phenylalanine transfer RNA that exhibits a K m of 2.6 x 10 -7 m . The enzyme is stable when stored at 4°.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)96232-0