Amino acid analog incorporation into bacterial proteins

The amino acid analogs norleucine and para-fluorophenylalanine are shown to be incorporated into the proteins of E. coli. Analysis of proteins by an ion-exchange column showed that the proteins formed in the presence of the analogs are not radically different molecular species but are physicochemica...

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Bibliographic Details
Published inBiochimica et biophysica acta Vol. 34; pp. 39 - 46
Main Authors Cowie, Dean B., Cohen, Georges N., Bolton, Ellis T., De Robichon-Szulmajster, Huguette
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.01.1959
Subjects
Amino Acids - metabolism
Amino Acids, Diamino
Bacterial Proteins
Dietary Proteins
Old Medline
Proteins - metabolism
PROTEINS/metabolism
AMINO ACIDS/metabolism
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Summary:The amino acid analogs norleucine and para-fluorophenylalanine are shown to be incorporated into the proteins of E. coli. Analysis of proteins by an ion-exchange column showed that the proteins formed in the presence of the analogs are not radically different molecular species but are physicochemically similar to the proteins normally synthesized. The substitution of norleucine for methionine in the bacterial proteins was shown to occur in the same proportions in all of the “protein classes” resolved by the ion-exchange column.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0006-3002
1878-2434
DOI:10.1016/0006-3002(59)90230-6