| Autor: |
HUISMAN, T. H. J., DOZY, A. M., NECHTMAN, C., THOMPSON, R. B. |
| Zdroj: |
Nature; September 1962, Vol. 195 Issue: 4846 p1109-1110, 2p |
| Abstrakt: |
EVIDENCE has been presented in a previous investigation1that the normally occurring minor hæmoglobin component A2has a considerably higher affinity for oxygen than normal Hb–A. The Hb–A2preparations, which were isolated by carboxymethyl-cellulose (CMC) chromatography2, however, contained relatively large quantities (up to 20 per cent) ferri–Hb or ferri–Hb derivatives. In the work reported here we redetermined, therefore, the oxygen equilibria of normal Hb–A0and Hb–A2, both being isolated as oxyhæmoglobin without notable oxidation to ferri-hæmoglobin derivatives. The abnormal variant of Hb–A2, known as Hb–A21or Hb–B2(ref. 3), has also been included in this work. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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