The Experts below are selected from a list of 261 Experts worldwide ranked by ideXlab platform
David S. Hage - One of the best experts on this subject based on the ideXlab platform.
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Affinity monolith chromatography
Journal of Separation Science, 2006Co-Authors: Rangan Mallik, David S. HageAbstract:The combined use of monolithic supports with selective Affinity ligands as stationary phases has recently given rise to a new method known as Affinity monolith chromatography (AMC). This review will discuss the basic principles behind AMC and examine the types of supports and ligands that have been employed in this method. Approaches for placing Affinity ligands in monoliths will be considered, including methods based on covalent immobilization, biospecific adsorption, entrapment, and the formation of coordination complexes. Several reported applications will then be presented, such as the use of AMC for bioAffinity chromatography, immunoAffinity chromatography, immobilized metal-ion Affinity chromatography, dye-ligand Affinity chromatography, and biomimetic chromatography. Other applications that will be discussed are chiral separations and studies of biological interactions based on AMC.
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Handbook of Affinity Chromatography, Second Edition - Handbook of Affinity chromatography
2005Co-Authors: David S. HageAbstract:INTRODUCTION AND BASIC CONCEPTS An Introduction to Affinity Chromatography D.S. Hage and P.F. Ruhn Support Materials for Affinity Chromatography P. Gustavsson and P. Larsson Immobilization Methods for Affinity Chromatography H.S. Kim and D.S. Hage Application and Elution in Affinity Chromatography D.S. Hage, H. Xuan, and M.A. Nelson GENERAL Affinity LIGANDS AND METHODS BioAffinity Chromatography D.S. Hage, M. Bian, R. Burks, E. Karle, C. Ohnmacht, and C. Wa ImmunoAffinity Chromatography D.S. Hage and T.M. Phillips DNA Affinity Chromatography R.A. Moxley, S. Oak, H. Gadgil, and H.W. Jarrett Boronate Affinity Chromatography X. Liu and W.H. Scouten Dye-Ligand and Biomimetic Affinity Chromatography N.E. Labrou, K. Mazitsos, and Y.D. Clonis Immobilized Metal-Ion Affinity Chromatography D. Todorova and M.A. Vijayalakshmi PREPARATIVE APPLICATIONS General Considerations in Preparative Affinity Chromatography A. Subramanian Affinity Chromatography of Enzymes F. Friedberg and A.R. Rhoads Isolation of Recombinant Proteins by Affinity Chromatography A. Subramanian Affinity Chromatography in Antibody and Antigen Purification T.M. Phillips Affinity Chromatography of Regulatory and Signal-Transducing Proteins A.R. Rhoads and F. Friedberg Receptor-Affinity Chromatography P. Bailon, M. Nachman-Clewner, C. L. Spence, and G.K. Ehrlich ANALYTICAL AND SEMIPREPARATIVE APPLICATIONS Affinity Methods in Clinical and Pharmaceutical Analysis Carrie A.C. Wolfe, W. Clarke and D.S. Hage Affinity Chromatography in Biotechnology N. Jordan and I. Krull Environmental Analysis by Affinity Chromatography M.A. Nelson and D.S. Hage Affinity Chromatography in Molecular Biology L.A. Jurado, S.Oak, Himanshu Gadgil, R.A. Moxley, and H.W. Jarrett Affinity-Based Chiral Stationary Phases S. Patel, I.W. Wainer and W.J. Lough BIOPHYSICAL APPLICATIONS Quantitative Affinity Chromatography: Practical Aspects D.S. Hage and J. Chen Quantitative Affinity Chromatography: Recent Theoretical Developments D.J. Winzor Chromatographic Studies of Molecular Recognition and Solute Binding to Enzymes and Plasma Proteins S. Patel, I.W. Wainer and W.J. Lough Affinity-Based Optical Biosensors S.D. Long and D.G. Myszka RECENT DEVELOPMENTS Affinity Ligands in Capillary Electrophoresis Niels H. H. Heegaard and C. Schou Affinity Mass Spectrometry C.J. Briscoe, W. Clarke and D.S. Hage Microanalytical Methods Based on Affinity Chromatography T.M. Phillips Chromatographic Immunoassays A.C. Moser and D.S. Hage Molecularly Imprinted Polymers: Artificial Receptors for Affinity Separations K. Haupt
Tanja Oswald - One of the best experts on this subject based on the ideXlab platform.
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purification of his 6ecorv recombinant restriction endonuclease ecorv fused to a his 6Affinity domain by metal chelate Affinity chromatography
Biotechnology and Applied Biochemistry, 1997Co-Authors: Tanja Oswald, Ursula Rinas, Gabi Hornbostel, Birger F AnspachAbstract:The chromatographic purification of (His) 6 EcoRV, a fusion protein consisting of a hexahistidine Affinity domain and restriction endonuclease EcoRV produced from recombinant Escherichia coli, led to high product concentrations (≥ I mg/ml) in the preparative mode. Increasing the amount of applied crude cell homogenate caused competition with host-specific proteins, leading to a decrease of recovery and purity of the fusion protein. Reduction of host-specific proteins was achieved by pre-adsorption on to a DEAE anion-exchange sorbent. This, in combination with 0.5-1 M NaCI in the adsorption buffer, assured a purity >95% and a total protein recovery of 34% in the preparative mode. Contamination of the product with about 2 mol of Ni(II)/mol of (His) 6 EcoRV was found due to metal-ion transfer to the N-terminal high-Affinity binding site at (His) 6 . Tris(carboxymethyl)ethylenediamine TED)-Sepharose was employed as an Ni(ll) adsorber. One passage of Ni(II)-contaminated protein solutions through the TED-Sepharose column resulted in a decrease in the Ni(ll) content in the (His) 6 EcoRV fractions below the detection limit ( 0.02 mg/l) of the atomic-adsorption spectrophotometer.
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Purification of (His)6EcoRV [recombinant restriction endonuclease EcoRV fused to a (His)6Affinity domain] by metal‐chelate Affinity chromatography
Biotechnology and applied biochemistry, 1997Co-Authors: Tanja Oswald, Ursula Rinas, Gabi Hornbostel, F. Birger AnspachAbstract:The chromatographic purification of (His) 6 EcoRV, a fusion protein consisting of a hexahistidine Affinity domain and restriction endonuclease EcoRV produced from recombinant Escherichia coli, led to high product concentrations (≥ I mg/ml) in the preparative mode. Increasing the amount of applied crude cell homogenate caused competition with host-specific proteins, leading to a decrease of recovery and purity of the fusion protein. Reduction of host-specific proteins was achieved by pre-adsorption on to a DEAE anion-exchange sorbent. This, in combination with 0.5-1 M NaCI in the adsorption buffer, assured a purity >95% and a total protein recovery of 34% in the preparative mode. Contamination of the product with about 2 mol of Ni(II)/mol of (His) 6 EcoRV was found due to metal-ion transfer to the N-terminal high-Affinity binding site at (His) 6 . Tris(carboxymethyl)ethylenediamine TED)-Sepharose was employed as an Ni(ll) adsorber. One passage of Ni(II)-contaminated protein solutions through the TED-Sepharose column resulted in a decrease in the Ni(ll) content in the (His) 6 EcoRV fractions below the detection limit ( 0.02 mg/l) of the atomic-adsorption spectrophotometer.
Julia E Rice - One of the best experts on this subject based on the ideXlab platform.
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proton Affinity of methyl nitrate less than proton Affinity of nitric acid
Journal of the American Chemical Society, 1992Co-Authors: Timothy J. Lee, Julia E RiceAbstract:Several state-of-the-art ab initio quantum mechanical methods were used to investigate the equilibrium structure, dipole moments, harmonic vibrational frequencies, and IR intensities of methyl nitrate, methanol, and several structures of protonated methyl nitrate, using the same theoretical methods as in an earlier study (Lee and Rice, 1992) of nitric acid. The ab initio results for methyl nitrate and methanol were found to be in good agreement with available experimental data. The proton Affinity (PA) of methyl nitrate was calculated to be 176.9 +/-5 kcal/mol, in excellent agreement with the experimental value 176 kcal/mol obtained by Attina et al. (1987) and less than the PA value of nitric acid. An explanation of the discrepancy of the present results with those of an earlier study on protonated nitric acid is proposed.
Maria D. Furlong - One of the best experts on this subject based on the ideXlab platform.
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Antibody Affinity maturation in selectively bred high and low-Affinity mice.
European Journal of Immunology, 2005Co-Authors: Michael W. Steward, Carolynne Stanley, Maria D. FurlongAbstract:: The Affinity of serum antibodies produced by selectively bred lines of mice [high Affinity, low Affinity, low nonmaturing (N/M)] injected with T-dependent [human serum albumin (HSA), dinitrophenylated bovine gamma-globulin (DNP-BGG)] and T-independent (DNP-Ficoll) antigens in saline and adjuvant has been determined. The lines of mice differ significantly in the Affinity of antibody produced to T-dependent antigens injected in saline but not to the T-independent antigen. Unlike mice of the high and low-Affinity lines, low-Affinity N/M mice failed to show Affinity maturation to HSA and DNP-BGG injected in Freund's incomplete adjuvant. However, low-N/M mice responded to DNP-Ficoll injected in adjuvant by the production of antibody of Affinity comparable to that produced in the other lines and with a similar maturation in Affinity. Carrier priming resulted in the suppression of anti-hapten antibody Affinity in all lines but low-N/M mice showed significantly greater suppression late in the response to challenge. Low doses of cyclophosphamide produced a significant increase in Affinity in low-N/M mice. These results suggest that the failure of low-N/M mice to show Affinity maturation results from increased suppressor T cell activity. The availability of the selectively bred mice provides a useful model for the detailed study of the cellular basis of the control of antibody Affinity maturation.
Birger F Anspach - One of the best experts on this subject based on the ideXlab platform.
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purification of his 6ecorv recombinant restriction endonuclease ecorv fused to a his 6Affinity domain by metal chelate Affinity chromatography
Biotechnology and Applied Biochemistry, 1997Co-Authors: Tanja Oswald, Ursula Rinas, Gabi Hornbostel, Birger F AnspachAbstract:The chromatographic purification of (His) 6 EcoRV, a fusion protein consisting of a hexahistidine Affinity domain and restriction endonuclease EcoRV produced from recombinant Escherichia coli, led to high product concentrations (≥ I mg/ml) in the preparative mode. Increasing the amount of applied crude cell homogenate caused competition with host-specific proteins, leading to a decrease of recovery and purity of the fusion protein. Reduction of host-specific proteins was achieved by pre-adsorption on to a DEAE anion-exchange sorbent. This, in combination with 0.5-1 M NaCI in the adsorption buffer, assured a purity >95% and a total protein recovery of 34% in the preparative mode. Contamination of the product with about 2 mol of Ni(II)/mol of (His) 6 EcoRV was found due to metal-ion transfer to the N-terminal high-Affinity binding site at (His) 6 . Tris(carboxymethyl)ethylenediamine TED)-Sepharose was employed as an Ni(ll) adsorber. One passage of Ni(II)-contaminated protein solutions through the TED-Sepharose column resulted in a decrease in the Ni(ll) content in the (His) 6 EcoRV fractions below the detection limit ( 0.02 mg/l) of the atomic-adsorption spectrophotometer.
