Expression and Biotinylation of a Mutant of the Transcarboxylase Carrier Protein from Propioni shermanii

Jank, Matthias M.; Bokorny, Stefan; Röhm, Klaus‐Heinrich; Berger, Stefan

doi:10.1006/prep.1999.1097

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Cited by 5 publications

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“…By fusing the biotin containing domain of the 1.3S subunit of the transcarboxylase of Propionibacterium shermanii (PSTCD) to a target protein, these researchers demonstrated that biotinylated proteins could be synthesized in the cytoplasm of simple organisms. In the prokaryotic P. shermanii, the PSTCD consists of 123 amino acids and is posttranslationally biotinylated at the ⑀-amino group of the lysine at position 89 (10).…”

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confidence: 99%

Metabolic Biotinylation of Secreted and Cell Surface Proteins from Mammalian Cells

Parrott

Barry

2001

Biochemical and Biophysical Research Communications

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mentioning

confidence: 99%

Metabolic Biotinylation of Secreted and Cell Surface Proteins from Mammalian Cells

Parrott

Barry

2001

Biochemical and Biophysical Research Communications

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Biotinylation reagents for the study of cell surface proteins

2008

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The extraordinarily stable, non-covalent interaction between avidin and biotin is one of the most commonly exploited tools in chemistry and biology. Methods for derivatization with biotin of a variety of molecules (in particular, proteins) have been introduced, in order to allow their efficient recovery, immobilization and detection with avidin-based reagents. The field has evolved very rapidly and the applications have become more and more sophisticated. Cell surface protein studies have enormously benefited from refinements of this technology. It is now possible to specifically biotinylate one single membrane protein or to fish out a membrane receptor bound to its ligand. The release of biotinylated molecules from the avidin-based reagents, however, may still represent a major problem, due to the stability of the complex. This review will examine the biotin-avidin technology for the study of cell surface proteins, discussing reagents and techniques as well as examples of applications in quantitative proteomics.

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Methylmalonyl-CoA carboxytransferase

Springer Handbook of Enzymes

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Expression and Biotinylation of a Mutant of the Transcarboxylase Carrier Protein from Propioni shermanii

Cited by 5 publications

References 10 publications

Metabolic Biotinylation of Secreted and Cell Surface Proteins from Mammalian Cells

Metabolic Biotinylation of Secreted and Cell Surface Proteins from Mammalian Cells

Biotinylation reagents for the study of cell surface proteins

Methylmalonyl-CoA carboxytransferase

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