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Defatted albumin adsorption

Figure 11. Enhancement of defatted albumin adsorption on Pellethane 2363-80A by binding to octadecyl residues. Symbols represent different derivatization runs. Figure 11. Enhancement of defatted albumin adsorption on Pellethane 2363-80A by binding to octadecyl residues. Symbols represent different derivatization runs.
Figure 5. Albumin adsorption isotherms on Silastic before and after fat removal from the albumin. Films were equilibrated at 37°C for 20 hrs at the depicted albumin concentration in O.OIM HEPES, 0.147M NaCl, 0.02% azide, pH 7.4 and then rinsed with buffer at room temperature by the dilution displacement technique. Fraction V albumin (NBC 2106) was used untreated or defatted with charcoal (see Table III... Figure 5. Albumin adsorption isotherms on Silastic before and after fat removal from the albumin. Films were equilibrated at 37°C for 20 hrs at the depicted albumin concentration in O.OIM HEPES, 0.147M NaCl, 0.02% azide, pH 7.4 and then rinsed with buffer at room temperature by the dilution displacement technique. Fraction V albumin (NBC 2106) was used untreated or defatted with charcoal (see Table III...
Figure 12. Effect of enhanced binding of defatted albumin to octadecyl residues on reduction of fibrinogen adsorption. Figure 12. Effect of enhanced binding of defatted albumin to octadecyl residues on reduction of fibrinogen adsorption.
Polymers of biomedical interest can be treated in order to covalently bind C18 analogs of aliphatic chains. The treatment enhances binding of defatted albumin in short-term exposure, and reduces fibrinogen adsorption, in proportion to enhancement of albumin adsorption. The treatment appears promising for general improvement of blood compatibility of a number of polymers. [Pg.312]


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