Copolymerization of recombinant Phascolopsisgouldii hemerythrin with human serum albumin for use in blood substitutes. (17th February 2017)

• Record Type: Journal Article
• Authors: Arkosi, Mariann; Scurtu, Florina; Vulpoi, Adriana; Silaghi-Dumitrescu, Radu; Kurtz, Donald
• Is Part Of: Artificial cells, nanomedicine, and biotechnology. Volume 45:Number 2(2017)
• Page Start: 218
• Page End: 223
• Publication Date: 2017-02-17
• Subjects: Hemerythrin -- human serum albumin -- hemoglobin -- blood substitutes -- oxygen transport; Artificial cells -- Periodicals; Nanotechnology -- Periodicals; Blood substitutes -- Periodicals; Tissue engineering -- Periodicals; Molecules -- Periodicals; Biotechnology -- Periodicals; 615.39
• DOI: 10.1080/21691401.2016.1269118
• Languages: English
• ISSNs: 2169-1401

Abstract

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.