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University of Illinois at Urbana-Champaign
Recombinant Hemoglobin Variants: Structure-Function Analysis and Oxygen Therapeutic Design
Abstract
dc:descriptionIn 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.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Biochemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Sanders, Kevin Eugene
- Contributors dc:contributor
-
- Sligar, Stephen G.
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI9912367
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/84898