Abstract
Hemoglobin-based blood substitutes are one of the options available to derive a resuscitating
fluid taking into account clinical and physiological demands. In this paper we investigated a
novel protein, Hb(αα,ββ) obtained as a combination of two homodimers α2 and β2 both derived
from a fusion gene containing two alfa chains or two beta chains respectively coupled via a
specific linker. The construct here described is thus a novel heterodimeric hemoglobin carrying
four heme groups. The protein cannot dissociate into dimers, as demonstrated by its absence of
reactivity versus haptoglobin, and is expected to have a relatively long circulating half-life. The
modification does not increase the autoxidation rate, but increases the oxygen affinity, due to a
destabilization of the T quaternary state. Characterization of the biochemical properties of this
protein in comparison with HbA is reported.
Lingua originale | English |
---|---|
pagine (da-a) | 1462-1470 |
Numero di pagine | 9 |
Rivista | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS |
Stato di pubblicazione | Pubblicato - 2008 |
Keywords
- blood substitutes
- gene fusion
- oxygen carrier
- protein engineering