Mechanism for nitric oxide release from S-nitrosylated hemoglobin by an internal electron transfer and development of nitrosylated hemoglobin-based blood substitutes
Hemoglobin is a blood protein, contained within the red blood cells, which has been implicated in the transport of nitric oxide (NO) due to the observation of naturally S-nitrosylated hemoglobin, HbSNO, in vivo. This thesis provides support for a mechanism by which free NO (gas) is released by cleav...
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| Format: | Dissertation |
| Language: | English |
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ProQuest Dissertations & Theses
01-01-2002
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| Online Access: | Get full text |
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| Summary: | Hemoglobin is a blood protein, contained within the red blood cells, which has been implicated in the transport of nitric oxide (NO) due to the observation of naturally S-nitrosylated hemoglobin, HbSNO, in vivo. This thesis provides support for a mechanism by which free NO (gas) is released by cleavage of the S-NO bond upon the addition of an electron, from the ferrous heme, as observed by 1H-NMR. The rate of release of NO from deoxygenated HbSNO was found to be as: kobs = 1.00 ± 0.12 × 10−4 s−1 . Cross-linked hemoglobin has been recognized as a viable oxygen carrier with few side effects. One of these side effects is the scavenging of free NO by coordination to the ferrous heme, resulting in vasoconstriction due to the depletion of free NO. To counter the effects of this scavenging, a nitrosylated form of cross-linked hemoglobin has been synthesized and its properties are reported. |
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| ISBN: | 0612686825 9780612686823 |