Copolymerization of recombinant Phascolopsisgouldii hemerythrin with human serum albumin for use in blood substitutes

Abstract

Hemerythrin is an oxygen-carrying protein found in marine invertebrates and may be a promising alternative to hemoglobin for use in blood substitutes, primarily due to its negligible peroxidative toxicity. Previous studies have shown that glutaraldehyde-induced copolymerization of hemoglobin with bovine serum albumin increases the half-life of the active oxy form of hemoglobin (i.e. decreases the auto-oxidation rate). Here, we describe a protocol for glutaraldehyde copolymerization of Hr with human serum albumin and the dioxygen-binding properties of the co-polymerized products. The copolymerization with HSA results in alteration of hemerythrin’s dioxygen-binding properties in directions that may be favorable for use in blood substitutes.

Keywords:

• Hemerythrin
• human serum albumin
• hemoglobin
• blood substitutes
• oxygen transport

Acknowledgements

Funding from the The Romanian Ministry of Education and Research (Grants PN09-440213 and PN-II-ID-PCE-2012-4-0488) is gratefully acknowledged. F. S. thanks the “Babes-Bolyai” University for the financial support via the Sectoral Operational Programme for Human Resources Development 2007–2013, co-financed by the European Social Fund, under the project POSDRU/159/1.5/S/132400 with the title “Young successful researchers – professional development in an international and interdisciplinary environment”. M. A. thanks the Babeş-Bolyai University for a student research scholarship. Augustin Mot and Denisa Hathazi (BBU, Department of Chemistry) are thanked for helpful discussions.

Disclosure statement

The authors declare no conflict of interest.

Additional information

Funding

The Romanian Ministry of Education and Research [grant PN-II-ID-PCE-2012-4-0488, grant PN09-440213]. ”Babeş-Bolyai” University via the Sectoral Operational Programme for Human Resources Development 2007-2013[POSDRU/159/1.5/S/132400].