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Affinity chromatography of neoglycoproteins
Bioseparation, 2000Glycoproteins, as a class of biomolecules, exhibit much more heterogeneous structures than non-glycosylated proteins. They present a challenging area of research. Model glycoproteins with well-defined protein and carbohydrate structures are helpful in the search for high-resolution methods for the separation of glycoproteins.
Y, Li +4 more
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Affinity chromatography of transaminases
Analytical Biochemistry, 1971Abstract It is shown that glutamic-oxaloacetic transaminase from pig heart can be selectively and reversibly bound to a Sepharose column substituted with N′-alkyl derivatives of pyridoxamine 5′-phosphate. A simple procedure is described which includes formation of apotransaminase, its binding to the substituted Sepharose, and its elution under the ...
R, Collier, G, Kohlhaw
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Shielding Affinity Chromatography
Bio/Technology, 1994Pulsing your columns with polymers prevents nonspecific binding and allows elution by temperature ...
I Y, Galaev, B, Mattiasson
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Molecular Biotechnology, 2001
DNA-affinity chromatography has been used for the purification of DNA-binding proteins that control various cellular processes. There have been improvements in coupling methods and choice of supports over the years. The procedure for coupling 5'-aminoethyl-(dT)18 to silica activated with N-hydroxysuccinimide and a carbodiimide has been described. Also,
P S, Chockalingam +2 more
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DNA-affinity chromatography has been used for the purification of DNA-binding proteins that control various cellular processes. There have been improvements in coupling methods and choice of supports over the years. The procedure for coupling 5'-aminoethyl-(dT)18 to silica activated with N-hydroxysuccinimide and a carbodiimide has been described. Also,
P S, Chockalingam +2 more
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Stress-Free Chromatography: Affinity Chromatography
Current Pharmaceutical Biotechnology, 2009A number of approaches are available in minimizing aggregation of the final protein products. This chapter describes one such approach, i.e., an attempt to avoid stressful conditions that may eventually lead to protein aggregation. Affinity chromatography uses specific interaction between protein to be purified and ligand attached to the column. Due to
Tsutomu, Arakawa +3 more
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Trypsin and affinity chromatography
Journal of Chromatography A, 1992Affinity adsorbents for trypsin which were prepared by immobilizing product-type ligands, that is, peptides having C-terminal arginine, proved to be effective not only for preparative purposes but also for basic research on molecular recognition. The properties of the binding site of trypsin were revealed by chromatographic experiments.
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Quantitative affinity chromatography
Journal of Biochemical and Biophysical Methods, 1997Abstract Quantitative affinity chromatography was introduced (1) at a stage when the preparative technique was well established as a method of solute purification, and has been developed to take additional advantage of the chromatographic matrix used for isolation of the solute on the basis of biospecificity.
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Current Protocols in Protein Science, 1995
AbstractDye affinity chromatography is a protein purification procedure based on the high affinity of immobilized dyes for the binding sites on many proteins. It is a rapid, inexpensive, and versatile method that is applicable to the purification of crude cellular extracts. This unit presents protocol for the three types of dye affinity chromatography:
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AbstractDye affinity chromatography is a protein purification procedure based on the high affinity of immobilized dyes for the binding sites on many proteins. It is a rapid, inexpensive, and versatile method that is applicable to the purification of crude cellular extracts. This unit presents protocol for the three types of dye affinity chromatography:
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Lectin Affinity Chromatography
Current Protocols in Protein Science, 1995AbstractThis unit describes the use of lectins for preparative glycoprotein purification. Con A‐Sepharose and WGA‐agarose are used for convenience and availability. Instructions are given for a small‐scale pilot procedure to test for lectin binding and to determine elution conditions.
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