Understanding the mechanism of hemoglobin dissociation and association is a fundamental factor to study hemoglobin stability and production of hemoglobin based extracellular oxygen carriers. Clinical studies with different crosslinked and modified hemoglobins reveled symptoms which are due to fast kidney filtration and accelerated autoxidation. We are utilizing ultrafast time-resolved intrinsic tryptophan fluorescence for monitoring the hemoglobin dissociation into the dimers and monomers under high hydrostatic pressure. Our study include native human hemoglobin as well as crosslinked and mutated human and bovine hemoglobins.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR008119-09
Application #
6444734
Study Section
Project Start
2001-04-01
Project End
2002-03-31
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
9
Fiscal Year
2001
Total Cost
$293,069
Indirect Cost
Name
University of Maryland Baltimore
Department
Type
DUNS #
003255213
City
Baltimore
State
MD
Country
United States
Zip Code
21201
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