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Updated: Jul 7, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
Published on: July 31, 2010
Hb(alphaalpha,betabeta): a novel fusion construct for a dimeric, four-domain hemoglobin
Gianna Panetta1, Alessandro Arcovito, Veronica Morea
1Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università di Roma "Sapienza", Piazzale A. Moro 5 00185 Roma, Italy.
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.
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