Recombinant Hemoglobin Variants: Structure-Function Analysis and Oxygen Therapeutic Design
Sanders, Kevin Eugene
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https://hdl.handle.net/2142/84898
Description
Title
Recombinant Hemoglobin Variants: Structure-Function Analysis and Oxygen Therapeutic Design
Author(s)
Sanders, Kevin Eugene
Issue Date
1998
Doctoral Committee Chair(s)
Sligar, Stephen G.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
Abstract
In a rat model each protein exhibited an increased vascular lifetime and no renal excretion. Furthermore, a dose dependent increase in vascular lifetime was observed suggesting that the protein clearance mechanism is saturatable. These circularly permuted variants represent the first recombinantly designed polymerized hemoglobin. The clear structural and functional similarity of these variants to native hemoglobin and improved vascular stability suggests that they have potential for use as an oxygen carrying therapeutic.
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