Synthesis of the protein cutting reagent iron (S)-1-(p- bromoacetamidobenzyl)ethylenediaminetetraacetate and conjugation to cysteine side chains

Bioconjugate Chemistry

Volumn 8, Issue 1, 1997, Pages 44-48

  Greiner, Douglas P ^a,b   Miyake, Reiko ^a   Moran, Justin K ^a,c   Jones, A Daniel ^a   Negishi, Tomofumi ^d   Ishihama, Akira ^d   Meares, Claude F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b GENENTECH INC   (United States)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^d NATIONAL INSTITUTE OF GENETICS   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CHAINS; CHELATION; ELECTROSPRAY IONIZATION; ESCHERICHIA COLI; MASS SPECTROMETRY; PEPTIDES;

CROSSLINKER; FLUORESCENT PROBES; HYDROLYSIS REACTION; IRON CHELATE; LABELING REAGENT; PEPTIDE BONDS; PEPTIDE HYDROLYSIS; PROTEIN LABELING; SIDE-CHAINS; SINGLE SITES;

IRON;

ESCHERICHIA COLI;

EID: 0031056514     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc9600731     Document Type: Article

References (13)

1. Rana, T. M., and Meares, C. F. (1990) Specific Cleavage of a Protein by an Attached Iron Chelate. J. Am. Chem. Soc. 112, 2457-2458.
2. Rana, T. M., and Meares, C. F. (1991) Transfer of Oxygen from an Artificial Protease to Peptide Carbon During Proteolysis. Proc. Natl. Acad. Sci. U.S.A. 88, 10578-10582.
3. Ermacora, M. R., Ledman, D. W., and Fox, R. O. (1996) Mapping the Structure of a Non-Native State of Staphylococcal Nuclease. Nat. Struct. Biol. 3, 59-66.
4. Ghaim, J. B., Greiner, D. P., Meares, C. F., and Gennis, R. B. (1995) Proximity Mapping the Surface of a Membrane Protein Using an Artificial Protease: Demonstration That the Quinone-Binding Domain of Subunit I Is near the N-Terminal Region of Subunit II of Cytochrome bd. Biochemistry 34, 11311-11315.
5. Sundberg, M. W., Meares, C. F., Goodwin, D. A., and Diamanti, C. I. (1974) Chelating Agents for the Binding of Metal Ions to Macromolecules. Nature (London) 250, 587-588.
6. DeRiemer, L. H., Meares, C. F., Goodwin, D. A., and Diamanti, C. I. (1981) BLEDTA II: Synthesis of a New Tumor-Visualizing Derivative of Co(III)-Bleomycin. J. Labelled Compd. Radiopharm. 18, 1517-1534.
7. Hayward, M. M., Adrian, J. C., Jr., and Schepartz, A. (1995) Convenient Synthesis of Bifunctional Metal Chelates. J. Org. Chem. 60, 3924-3927.
8. Thiers, R. C. (1957) Contamination in Trace Element Analysis and Its Control. Methods Biochem. Anal. 5, 273-335.
9. Moran, J. K., Greiner, D. P., and Meares, C. F. (1995) Improved Synthesis of 6-[p-(Bromoacetamido)benzyl]-1,4,8, 11-tetraazacyclotetradecane-N,N′,N″,N‴-tetraacetic Acid and Development of a Thin-Layer Assay for Thiol-Reactive Bifunctional Chelating Agents. Bioconjugate Chem. 6, 296-301.
10. Jeon, Y. H., Negishi, T., Shirakawa, M., Yamazaki, T., Fujita, N., Ishihama, A., and Kyogoku, Y. (1995) Solution Structure of the Activator Contact Domain of the RNA Polymerase Alpha Subunit. Science (Washington, D.C.) 270, 1495-1497.
11. Parvari, R., Pecht, I., and Soreq, H. (1983) A Microfluorometric Assay for Cholinesterases, Suitable for Multiple Kinetic Determinations of Picomoles of Released Thiocholine. Anal. Biochem. 133, 450-456.
12. Heyduk, E., and Heyduk, T. (1994) Mapping Protein Domains Involved in Macromolecular Interactions: A Novel Protein Footprinting Approach. Biochemistry 33, 9643-9650.
13. 70 Protein to the Core Subunits of Escherichia coli RNA Polymerase, Studied by Iron-EDTA Protein Footprinting. Proc. Natl. Acad. Sci. U.S.A. 93, 71-75.