| Autor: |
McGown EL; Blood Research Division, Letterman Army Institute of Research, Presidio of San Francisco, California 94129., Dill K, O'Connor RJ, Khan M, LeTellier YC, Vandegriff KD |
| Jazyk: |
angličtina |
| Zdroj: |
Analytical biochemistry [Anal Biochem] 1992 Nov 15; Vol. 207 (1), pp. 85-9. |
| DOI: |
10.1016/0003-2697(92)90505-2 |
| Abstrakt: |
Functional hemoglobin was regenerated from partially autoxidized hemoglobin by reduction with molecular hydrogen in the presence of a heterogeneous catalyst consisting of elemental platinum embedded in an electroactive polymer. The visible spectrum of the regenerated hemoglobin was identical to that of native iron(II) hemoglobin. The regenerated hemoglobin displayed highly cooperative oxygen-binding characteristics. P50 values for oxidized-regenerated hemoglobin samples were not different from native hemoglobin. The Hill coefficients for regenerated hemoglobin were slightly lower than the controls, possibly because of small amounts of irreversibly oxidized hemoglobin arising during the initial autoxidation. The advantages of the reduction system include: (1) the heterogeneous catalyst avoids the problem of protein adsorption onto bare platinum, (2) catalyst and reducing agent are easily removed from the protein, and (3) the by-product H+ is buffered easily. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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