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(alphaalpha,betabeta) obtained as a combination of two homodimers alpha(2) and beta(2) both derived from a fusion gene containing two alfa chains or two beta chains, each 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.

Hb(alphaalpha,betabeta): a novel fusion construct for a dimeric, four-domain hemoglobin / Panetta, Gianna; Arcovito, Alessandro; V., Morea; Bellelli, Andrea; Miele, Adriana Erica. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - STAMPA. - 1784:10(2008), pp. 1462-1470. [10.1016/j.bbapap.2008.01.003]

Hb(alphaalpha,betabeta): a novel fusion construct for a dimeric, four-domain hemoglobin.

PANETTA, GIANNA;ARCOVITO, Alessandro;BELLELLI, Andrea;MIELE, Adriana Erica
2008

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(alphaalpha,betabeta) obtained as a combination of two homodimers alpha(2) and beta(2) both derived from a fusion gene containing two alfa chains or two beta chains, each 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.
blood replacement; hemoglobin; site directed mutagenesis
01 Pubblicazione su rivista::01a Articolo in rivista
Hb(alphaalpha,betabeta): a novel fusion construct for a dimeric, four-domain hemoglobin / Panetta, Gianna; Arcovito, Alessandro; V., Morea; Bellelli, Andrea; Miele, Adriana Erica. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - STAMPA. - 1784:10(2008), pp. 1462-1470. [10.1016/j.bbapap.2008.01.003]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/105533
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