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Lectin affinity separation

Mullerschulte, D. and Daschek, W., Application of radiation grafted media for lectin affinity separation and urease immobilization—A novel-approach to tumor-therapy and renal-disease diagnosis, Radiat. Phys. Chem., 46, 1043, 1995. [Pg.979]

Glucose oxidase, glycoproteins from plasma membranes of rat liver Analytical and semi preparative separations Lectin Affinity (Concanavalin A) disks [76]... [Pg.75]

Fig. 3a. Flow diagram for the separation of the components of a complex mixture of oligosaccharides by serial lectin affinity chromatography. Depending upon the lectin adsorbant, specific oligosaccharides are either unbound (not retarded by the adsorbant), retarded (and eluted without the need of a saccharide inhibitor), or are tightly bound and then require either lOmM methyl a-D-glucopyranoside or lOOmM methyl a-D-mannopyranoside for elution. Where appropriate, each eluted peak is concentrated and the saccharide inhibitor is removed prior to application to the second affinity column. The structures of the individual oligosaccharides are shown in Fig. 3b. (Adapted from ref 288.)... Fig. 3a. Flow diagram for the separation of the components of a complex mixture of oligosaccharides by serial lectin affinity chromatography. Depending upon the lectin adsorbant, specific oligosaccharides are either unbound (not retarded by the adsorbant), retarded (and eluted without the need of a saccharide inhibitor), or are tightly bound and then require either lOmM methyl a-D-glucopyranoside or lOOmM methyl a-D-mannopyranoside for elution. Where appropriate, each eluted peak is concentrated and the saccharide inhibitor is removed prior to application to the second affinity column. The structures of the individual oligosaccharides are shown in Fig. 3b. (Adapted from ref 288.)...
Fragment separation hrPAGE PAGE, HPLC, 2DE HPLC, lectin affinity... [Pg.516]

A completely different approach, based on lectin-affinity CE was used by Bergstrom et al. [117] to separate AGP fractions. As mentioned in a previous section, using Con A as affinity ligand, they separated AGP into two peaks according to the biantennary content of the glycoforms. They applied this methodology to two AGP samples from patients with severe RA and one sample from a healthy donor. They found that the RA samples showed a decrease in the relative peak area of the biantennary peak compared with normal AGP. [Pg.686]

Sixteen glycoproteins have been separated from rat brain by a combination of hydroxyapatite and lectin affinity chromatography. A simple reproducible procedure for the fractionation of brain glycoproteins using hydroxyapatite-gel column chromatography has been developed. ... [Pg.365]

Putnam, D.D. Namasivayam, V. Bums, M.A. Cell affinity separations using magnetical stabilized fluidized beds Er5dbrocyte subpopulation fractionation utilization a lectin-magnetite support. Biotecbnol. Bioeng. 2003, 81, 650. [Pg.377]

Lectin affinity chromatography is a form of affinity chromatography where lectins are used to separate components within the sample. Lectins, such as Concanavalin A are proteins which can bind specific carbohydrate (sugar) molecules. The most common application is to separate proteins based on their Glycosylation groups. [Pg.64]

Fig. 8. The ARMES process with the forward extraction involving affinity interaction between a lectin (Con A) and a glycoprotein to separate from a mixture of glycoproteins and back extraction involving recovery of glycoprotein into an aqueous stripping phase. (Reproduced from [188] with permission of AIChE)... Fig. 8. The ARMES process with the forward extraction involving affinity interaction between a lectin (Con A) and a glycoprotein to separate from a mixture of glycoproteins and back extraction involving recovery of glycoprotein into an aqueous stripping phase. (Reproduced from [188] with permission of AIChE)...

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See also in sourсe #XX -- [ Pg.597 ]




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Affinity separation

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