Results 291 to 300 of about 539,588 (346)
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Shielding Affinity Chromatography

Bio/Technology, 1994
Pulsing your columns with polymers prevents nonspecific binding and allows elution by temperature ...
I Y, Galaev, B, Mattiasson
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Weak-affinity chromatography

Nature, 1990
Weak-affinity chromatography is a new method using readily reversible biospecific recognition as the basis for chromatographic separations.
Sten Ohlson, David Zopf
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DNA Affinity Chromatography

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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Affinity monolith chromatography

Journal of Separation Science, 2006
AbstractThe 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.
Rangan, Mallik, David S, Hage
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Stress-Free Chromatography: Affinity Chromatography

Current Pharmaceutical Biotechnology, 2009
A 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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Quantitative affinity chromatography

Journal of Biochemical and Biophysical Methods, 1997
Abstract 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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Dye Affinity Chromatography

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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Lectin Affinity Chromatography

Current Protocols in Protein Science, 1995
AbstractThis 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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Histidine Ligand Affinity Chromatography

Molecular Biotechnology, 1996
The sorbents with immobilized histidine as a pseudo affinity ligand with a wide specificity is described. The possibilities and relevant chemistries to use both particulate and flat or hollow fiber membranes as support matrices are discussed. The usefulness of such adsorbents for the purification of a wide variety of proteins, with relevant interaction
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Affinity Chromatography

Die Angewandte Makromolekulare Chemie, 1978
AbstractA decade and a half after its introduction, affinity chromatography, a method of purification based on biological recognition, has become a major means for the purification of biologically active molecules. Despite the enormous expansion of the field and the variety of biologically active materials that have been purified, the general approach ...
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