| Autor: |
Gribnau, T., Eekelen, C., Tesser, G., Nivard, R. |
| Zdroj: |
Journal of Solid Phase Biochemistry; 1978, Vol. 3 Issue 4, p271-289, 19p |
| Abstrakt: |
The synthesis of a biospecific adsorbent for trypsin was chosen as a model to investigate the applicability of FCP activation in affinity chromatography. p-Aminobenzamidine was chosen as a ligand, directly suitable for immobilization. The nonspecific binding properties of the first series of synthesized agarose derivatives were obviated either by FCP activation of the ligand instead of the matrix, or by modifying the initial FCP-activation procedure. The adsorbents prepared in this way, however, demonstrated no selectivity between trypsin and chymotrypsin. The introduction of e-aminocaproic acid as a spacer was ineffectual. These problems were solved by the application of glycylglycine as a spacer. The final affinity matrices had a degree of substitution of approximately 4 μ.mol of ligand per gram gel (100 μmol ligand per gram dry adsorbent). The specific activity of a current trypsin preparation was increased by 58% in a single cycle. The biospecificity of these adsorbents was demonstrated. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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