Results 211 to 220 of about 308,818 (265)
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Affinity chromatography of glycosyltransferases

Journal of Chromatography A, 1981
This review summarizes the use of biospecific chromatography techniques in the purification of mammalian glycosyltransferases. Ligands that are analogues of donor or acceptor substrates have been linked to cyanogen bromide-activated agarose for use as affinity adsorbents.
J E, Sadler, T A, Beyer, R L, Hill
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Affinity chromatography of phosphofructokinase

Archives of Biochemistry and Biophysics, 1976
Abstract 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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Affinity chromatography of neoglycoproteins

Bioseparation, 2000
Glycoproteins, 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, 1971
Abstract 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, 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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Trypsin and affinity chromatography

Journal of Chromatography A, 1992
Affinity 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, 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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"Affinity" Chromatography

Science, 1976
A D, Landman, E T, Pritchard
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Affinity Chromatography

Vox Sanguinis, 1972
I, Parikh, P, Cuatrecasas
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