Modification of hemoglobin with site-directed bifunctional reagents

M. P. Kavanaugh, D. T.B. Shih, R. T. Jones

Research output: Contribution to journalArticlepeer-review

Abstract

Reaction of deoxy-Hb with the periodate-oxidized derivatives of nicotinamide adenine dinucleotide (o-NAD), phosphoribosyl pyrophosphate (o-PRPP), adenosine triphosphate (o-ATP), glucose-1-phosphate (o-glc-1-P) and nicotinamide adenine dinucleotide phosphate (o-NADP) led to formation of cross-link adducts in varying yields as determined by SDS-polyacrylamide gel electrophoresis. Oxygen equilibrium studies were performed on Hb's cross-linked with o-NAD, o-PRPP and o-ATP. These derivatives were found to have increased oxygen affinity and were cross-linked between the β chains. Inositol hexaphosphate (IHP) blocked modification by these reagents, suggesting that modification was occurring in the organic phosphate binding site. In addition, it was found that the bifunctional reagent 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS) also led to formation of Hb cross-linked between the β chains, but resulted in a derivative with a dramatically decreased oxygen affinity, properties making it a potential candidate as an Hb-based cell-free blood substitute.

Original languageEnglish
Pages (from-to)99-104
Number of pages6
JournalActa Haematologica
Volume78
Issue number2-3
DOIs
StatePublished - 1987

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