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Original Article

Introduction of Negative Charges to a Crosslinked Hemoglobin: Lack of Effect on Plasma Half Time

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Pages 309-314 | Published online: 11 Jul 2009
 

Abstract

Intramolecularly crosslinked hemoglobins do not dissociate into α1β1 dimers. As a result, they escape glomerular filtration and have plasma half times of 4 hours. This value is shorter than for albumin (5.2 hours) with similar molecular weight but higher negative charge. The present study was done to determine if increased negative charge on a hemoglobin covalently crosslinked with bis (3,5-dibromosalicyl) sebacate would lengthen its plasma half time. Negative charge was introduced by acylation with succinic anhydride. The product had a higher negative charge; however, plasma half time was not increased. A larger fraction of the succinylated material was excreted in the urine suggesting molecular instability.

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