Results 121 to 130 of about 26,609 (166)

The oxygen affinity of sickle hemoglobin

Respiratory Physiology & Neurobiology, 2008
The right-shifted oxyhemoglobin dissociation curve of sickle cell disease (SCD) has been thought to result in abnormally low arterial oxygen saturation (S(o)(2)), even when oxygen partial pressure (P(o)(2)) is normal. However, without polymer formation (minimal under normoxic conditions), HbS oxygen affinity is normal.
Amgad, Abdu, José, Gómez-Márquez, Thomas K, Aldrich   +2 more
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Fetal Hemoglobin, Sickling, and Sickle Cell Disease

Advances in Pediatrics, 1990
Increased numbers of F cells and large amounts of Hb F/F cell appear to produce clinical benefit in rare variants of sickle cell disease and probably in more commonly encountered patients. Fetal hemoglobin interferes with polymerization of Hb S in vitro, but laboratory studies carried out with homogeneous hemoglobin solutions are inadequate models of ...
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Sickle Cell Hemoglobin Polymerization

1990
Publisher Summary The chapter describes the understanding of the physics and physical chemistry of sickle cell hemoglobin polymerization in solutions and in red cells. The polymerization of sickle cell hemoglobin has probably become the best understood of all protein self-assembly systems.
W A, Eaton, J, Hofrichter
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Plasma Hemoglobin and Hemoglobin Fractions in Sickle Cell Crisis

American Journal of Clinical Pathology, 1971
The geometric mean of plasma hemoglobin concentrations assayed by a modified benzidine procedure in 14 patients with sickle cell anemia (S-S hemoglobin) during 18 painful crises was 8.5 mg. per 100 ml. as compared with 5.9 mg. per 100 ml. during quiescent periods and 0.3 mg. per 100 ml. in normal controls. On the first and second days of crisis, plasma
H N, Naumann, L W, Diggs, L, Barreras, B J, Williams   +3 more
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A Novel Sickle Hemoglobin: Hemoglobin S-South End

Journal of Pediatric Hematology/Oncology, 2004
Sickle hemoglobin (Hb S; beta Glu6Val) is due to an AGTG; beta Lys132Asn, AAA>AAC). When present alone, the beta Lys132Asn mutation has low oxygen affinity. Therefore, this mutation may enhance the polymerization of the Hb S variant. Furthermore, the variant hemoglobin mimics Hb A on high-pressure liquid chromatography, and its identity is not easily ...
Hong-Yuan, Luo, Adeboye H, Adewoye, Shawn H, Eung, Timothy P, Skelton, Karen, Quillen, Lillian, McMahon, Martin H, Steinberg, David H K, Chui   +7 more
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Interactions between sickle hemoglobin fibers

Faraday Discussions, 2002
We report on observations of "zippering" that occurs when two sickle hemoglobin fibers come together side by side. A transient Y-shaped object is formed which "zips " closed. We have been able to show how the strength of the interactions that drive this may be estimated by studying the frustrated structures sometimes formed between several fibers.
Christopher W, Jones, Jiang Cheng, Wang, Frank A, Ferrone, Robin W, Briehl, Matthew S, Turner   +4 more
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Sickle Hemoglobin Fibers: Mechanisms of Depolymerization

Journal of Molecular Biology, 2002
We examined the depolymerization of hemoglobin (Hb) S fibers in the presence of CO by using photolysis of COHbS to create and isolate individual fibers, then removing photolysis to induce depolymerization. Depolymerization occurs at two sites, fiber ends and fiber sides, with different kinetics and by different mechanisms. At low partial pressure of CO
Gunjan, Agarwal, Jiang Cheng, Wang, Suzanna, Kwong, Scott M, Cohen, Frank A, Ferrone, Robert, Josephs, Robin W, Briehl   +6 more
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Interactions of Other Hemoglobin Variants with Sickle-Cell Hemoglobin

New England Journal of Medicine, 1970
Deoxygenation-induced sickling of erythrocytes and gelling of hemolysates containing sickle-cell hemoglobin (Hb) are manifestations of the tendency of deoxyhemoglobin S in concentrated solutions to aggregate with the formation of gels or tactoids (liquid crystals).
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Stereospecific Inhibitors of the Gelation of Sickle Hemoglobin

Hemoglobin, 1980
During the last decade there have been major advances in understanding the structure of the gel of deoxyhemoglobin S and the mechanism of its formation. These advances have allowed the development of a new strategy for the inhibition of gelation, i.e., stereospecific competitive inhibitors of the polymerization process.
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The Neurotoxic Effect of Sickle Cell Hemoglobin

Free Radical Research, 2004
A growing body of experimental evidence suggests that the oxidative neurotoxicity of hemoglobin A may contribute to neuronal loss after CNS hemorrhage. Several hemoglobin variants, including hemoglobin S, are more potent oxidants in cell-free systems.
Garig M, Vanderveldt, Raymond F, Regan
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