Subunit dissociation of certain abnormal human hemoglobins
AUTOR(ES)
Bunn, H. Franklin
RESUMO
The extent of dissociation of various hemoglobins into subunits was estimated from their elution volumes (Ve) on G-100 Sephadex. Under the same controlled conditions carboxyhemoglobins A, A3 (A1), F, S, and C all had the same elution volumes. The carboxy and cyanmet derivatives of hemoglobin Kansas (a variant with very low oxygen affinity) had a relatively high Ve, indicating a decreased mean molecular weight and therefore an increased tendency to form dimers and even monomers. Conversely, the liganded derivatives of hemoglobin Chesapeake (a variant with high oxygen affinity) had a relatively low Ve, suggestive of an impaired degree of subunit dissociation. Deoxyhemoglobin Chesapeake had a Ve identical with that of deoxyhemoglobin A. Cat hemoglobin, known to have an unusually low oxygen affinity, was found to have a higher Ve than human, dog, rabbit, rat, or guinea pig hemoglobins.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=322198Documentos Relacionados
- ON DISSOCIATION AND RECOMBINATION OF HUMAN ADULT HEMOGLOBINS A, S, AND C
- STUDIES OF THE INCORPORATION OF Fe59 INTO NORMAL AND ABNORMAL HEMOGLOBINS*
- The Linkage Between Oxygenation and Subunit Dissociation in Human Hemoglobin
- Heterometallic hybrids of homometallic human hemoglobins.
- A Survey of Hemoglobins, Transferrins and Certain Red Cell Antigens in Nine Breeds of Sheep