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Affinity chromatography of phosphofructokinase
Archives of Biochemistry and Biophysics, 1976Abstract The behavior of mammalian phosphofructokinase on immobilized adenine nucleotides was investigated. Three different insolubilized ligands were compared using a pure rabbit muscle phosphofructokinase. N 6 -[(6-aminohexyl)-carbamoyl-methyl]-ATP-Sepharose bound at least 90 times more enzyme than either N 6 -(6-aminohexyl)-AMP-agarose or ATP ...
C S, Ramadoss, L J, Luby, K, Uyeda
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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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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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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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