Specific N-terminal biotinylation of a protein in vitro by a chemically modified tRNAfmet can support the native activity of the translated protein

Journal of Bioscience and Bioengineering

Volumn 92, Issue 2, 2001, Pages 149-153

  Taki, Masumi ^a   Sawata, Shinya Y ^a   Taira, Kazunari ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Escherichia coli initiator tRNAfmet; Fluorescence imaging; Green fluorescent protein (GFP); In vitro translation; Monomeric streptavidin; N terminal biotinylation; Native activity

Indexed keywords

CHEMICAL MODIFICATION; CHROMATOGRAPHY; DENSITOMETERS; ESCHERICHIA COLI; FLUORESCENCE; RNA;

BIOTINYLATION;

PROTEINS;

GREEN FLUORESCENT PROTEIN; METHIONINE; TRANSFER RNA;

AFFINITY CHROMATOGRAPHY; AMINO TERMINAL SEQUENCE; AMINOACYLATION; ARTICLE; BIOTINYLATION; CHEMICAL MODIFICATION; COLUMN CHROMATOGRAPHY; DENSITY; FLUORESCENCE; IN VITRO STUDY; NONHUMAN; PROTEIN ANALYSIS; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; RNA TRANSLATION; WESTERN BLOTTING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034854557     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.92.149     Document Type: Article

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