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Lectin Affinity Chromatography

2023
Glycosylation is a non-template-driven posttranslational modification during which linked-sugars and glycans are added to the nascent polypeptide. Over 70% of the eukaryotic proteome is thought to be glycosylated. It is now known that correct glycosylation is essential for the correct folding, solubility, stability, and immunogenicity of proteins.
Brendan F, O'Connor   +2 more
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Lectin Affinity Chromatography

Molecular Biotechnology, 1994
Lectins are glycoproteins or proteins that have a selective affinity for a carbohydrate, or a group of carbohydrates. Many purified lectins are readily available and these maybe immobilized to a variety of chromatography supports.
I, West, O, Goldring
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Affinity Chromatography And Metal Chelate Affinity Chromatography

C R C Critical Reviews in Analytical Chemistry, 1987
The extremely rapid growth in the field of protein chemistry during the past 50 years has been due in large part to the development of very effective techniques of protein separation and analysis. A number of techniques such as electrophoresis or isoelectric focusing, based on the overall charge and mass of a biomolecule, have been widely applied ...
Alexander J. Fatiadi, L. Anderson
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Centrifugal affinity chromatography

Journal of Chromatography A, 1990
A new technique termed centrifugal affinity chromatography (CAC) is presented in this paper. CAC combines a high flow-rate, created by centrifugal force, with the specificity of affinity chromatography. This technique has been used for the purification of human immunoglobulin G.
R J, Slingerland   +2 more
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Receptor Affinity Chromatography

Annals of the New York Academy of Sciences, 1985
Insulin receptor was purified in high yield from cultured 3T3-L1 mouse adipocytes using the bifunctional ligand N alpha B1-(biotinyl-epsilon-aminocaproyl)insulin in conjunction with avidin-Sepharose CL-4B. This ligand is 100% competent as insulin and 60% competent as biotin, as measured by competitive binding assays.
R A, Kohanski, M D, Lane
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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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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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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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