Related Articles1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells.
Biophys J. 1995 Feb;68(2):681-93
Authors: Fetler BK, Simplaceanu V, Ho C
Using improved selective excitation methods for protein nuclear magnetic resonance (NMR), we have conducted measurements of the oxygenation of hemoglobin inside intact human red blood cells. The selective excitation methods use pulse shape-insensitive suppression of the water signal, while producing uniform phase excitation in the region of interest and, thus, are suitable for a wide variety of applications in vivo. We have measured the areas of 1H-NMR resonances of the hyperfine-shifted, exchangeable N delta H protons of the proximal histidine residues of the alpha- and beta-chains in deoxyhemoglobin (63 and 76 ppm downfield from the proton resonance of 2,2-dimethyl-2-silapentane-5-sulfonate (DSS), respectively), which are sensitive to the paramagnetic state of the iron, and for which the alpha- and beta-chain resonances are resolved, and from the ring current-shifted gamma 2-CH3 protons of the distal valine residues in oxyhemoglobin (2.4 ppm upfield from DSS), which are sensitive to the conformation of the heme pocket in the oxy state. We have found that the proximal histidine resonances are directly correlated with the degree of oxygenation of hemoglobin, whereas the distal valine resonances appear to be correlated with the conformation in the heme pocket that occurs after the binding of oxygen, in both the presence and absence of 2,3-diphosphoglycerate. In addition, from the proximal histidine resonances, we have observed a preference for the binding of oxygen to the alpha-chain (up to about 10%) of hemoglobin over the beta-chain in both the presence and absence of 2,3-diphosphoglycerate. These new results obtained in intact erythrocytes are consistent with our previous 1H-NMR studies on purified human normal adult hemoglobin. A unique feature of our 1H-NMR method is the ability to monitor the binding of oxygen specifically to the alpha- and beta-chains of hemoglobin both in solution and in intact red blood cells. This information is essential to our understanding of the molecular basis for the hemoglobin molecule serving as the oxygen carrier in vertebrates.
(1)H NMR study of monocrotaline and its metabolites in human blood.
(1)H NMR study of monocrotaline and its metabolites in human blood.
(1)H NMR study of monocrotaline and its metabolites in human blood.
Food Chem Toxicol. 2011 Aug 6;
Authors: Yang YC, Crowder J, Wardle NJ, Yang L, White KN, Wang ZT, Annie Bligh SW
Monocrotaline (MCT) is a naturally occurring hepatotoxic pyrrolizidine alkaloid found in plants. This investigation is aimed at furthering the understanding of the role of blood in mediating the transport of MCT and its reactive metabolites in humans. Reactions of monocrotaline and its metabolites,...
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Changes in the NMR metabolic profile of human microglial cells exposed to lipopolysaccharide or morphine.
Changes in the NMR metabolic profile of human microglial cells exposed to lipopolysaccharide or morphine.
Changes in the NMR metabolic profile of human microglial cells exposed to lipopolysaccharide or morphine.
J Neuroimmune Pharmacol. 2010 Dec;5(4):574-81
Authors: El Ghazi I, Sheng WS, Hu S, Reilly BG, Lokensgard JR, Rock RB, Peterson PK, Wilcox GL, Armitage IM
Microglial cells play a major role in host defense of the central nervous system. Once activated, several functional properties are up-regulated including migration, phagocytosis, and...
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[NMR paper] NMR study of the sites of human hemoglobin acetylated by aspirin.
NMR study of the sites of human hemoglobin acetylated by aspirin.
Related Articles NMR study of the sites of human hemoglobin acetylated by aspirin.
Biochim Biophys Acta. 1999 Jul 13;1432(2):333-49
Authors: Xu AS, Macdonald JM, Labotka RJ, London RE
Acetylation of hemoglobin by aspirin and other acetylating agents has been used to generate hemoglobin analogs with altered structural and functional properties, and may prove useful in the treatment of sickle cell disease. We have studied the acetylation of human hemoglobin using acetylsalicylic...
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[NMR paper] Kinetics of choline transport and phosphorylation in human breast cancer cells; NMR a
Kinetics of choline transport and phosphorylation in human breast cancer cells; NMR application of the zero trans method.
Related Articles Kinetics of choline transport and phosphorylation in human breast cancer cells; NMR application of the zero trans method.
Anticancer Res. 1996 May-Jun;16(3B):1375-80
Authors: Katz-Brull R, Degani H
The mechanism and kinetics of choline transport and phosphorylation in MCF7 human breast cancer cells was studied by 31P, 13C and 2H NMR, applying the zero trans method. Choline was transported by a...
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[NMR paper] 1H NMR studies of reactions of copper complexes with human blood plasma and urine.
1H NMR studies of reactions of copper complexes with human blood plasma and urine.
Related Articles 1H NMR studies of reactions of copper complexes with human blood plasma and urine.
Biochem Pharmacol. 1992 Jan 22;43(2):137-45
Authors: Bligh SW, Boyle HA, McEwen AB, Sadler PJ, Woodham RH
Reactions of the copper complexes Cu(II)Cl2, 2-, and + (where DIPS is 3,5-diisopropylsalicylate and DMP is 2,9-dimethylphenanthroline) with human blood plasma and urine have been studied by 500 MHz 1H NMR spectroscopy, and CD spectroscopy has been used to...
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08-21-2010 11:41 PM
[NMR paper] Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the inte
Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the gadolinium(III) bis(m-boroxyphenylamide)diethylenetriaminepentaacetic acid complex with human oxygenated and deoxygenated hemoglobin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the...