Biotinylation of proteins

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Chemical modification or the reaction product thereof – e.g.,...

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530300, 530345, 530350, C07K 1900, C07K 200, C07K 1400

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active

057235848

ABSTRACT:
Biotinylation peptides can be fused to other peptides or proteins of interest using recombinant DNA techniques to provide efficient methods for biotinylating the resulting fusion proteins in vivo or in vitro.

REFERENCES:
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Cress et al., "Purification: a one-step nondenaturing purification method for recombinant proteins produced in E. Coli," 1993, Promega Notes 42:2-7.
Cronan, "The E. Coli bio Operon: Transcriptional Repression by an Essential Protein Modification Enzyme," 11 Aug. 1989, Cell 58:427-429.
Cronan, "Biotination of Proteins in Vivo," 25 Jun. 1990, J. Biol. Chem. 265(18):10327-10333.
Freytag et al., "Molelcualr cloning of a cDNA for human pyruvate carboxylase," J. Biol. Chem. 259:12831-12837 (1984).
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Schatz, Peter J., "Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli," Bio/Technology 11:1138-1143 (1993).
Shenoy et al., "Effect of mutations at Met-88 and Met-90 on the biotination of Lys-89 of the apo 1.3S subunit of transcarboxylase," FASEB J. 2(9):2505-2511.
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