Sickle hemoglobin (HbS) reconstituted with Ni(II) protoporphyrin IX (Ni(II)HbS) can serve as a useful model for studying the polymerization of HbS and the effect of antisickling agents on gelation. Ni(II)HbS exist in the deoxy-like conformational state, does not bind 02, is not oxidized by 02 and is not photolabile. Thus, Ni(II) HbS is well suited for studies which are extremely difficult using native deoxy HbS. The utility of Ni(II)Hbs as a model could further our understanding of the polymerization process and increase ones ability to design drugs to effectively treat Sickle Disease. Ni(II)HbS and hybrids will be studied by Electron Microscopy (EM), Proton Nuclear Magnetic Resonance (NMR), Solubility (Csat) and Temperature Jump Gelation Kinetics in the absence and presence of antisickling agents. These studies will allow for a detailed assessment of Ni(II)HbS as a model for native deoxy HbS.

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Unknown (R23)
Project #
5R23HL032404-03
Application #
3448641
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1984-07-01
Project End
1987-06-30
Budget Start
1986-07-01
Budget End
1987-06-30
Support Year
3
Fiscal Year
1986
Total Cost
Indirect Cost
Name
Benedict College
Department
Type
Schools of Arts and Sciences
DUNS #
073727943
City
Columbia
State
SC
Country
United States
Zip Code
29204