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Sickle Cell Hemoglobin

2020
Sickle cell hemoglobin (HbS) is an example of a genetic variant of human hemoglobin where a point mutation in the β globin gene results in substitution of glutamic acid to valine at sixth position of the β globin chain. Association between tetrameric hemoglobin molecules through noncovalent interactions between side chain residue of βVal6 and ...
Amit Kumar, Mandal   +2 more
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Alternative diaspirins for modification of hemoglobin and sickle hemoglobin

Archives of Biochemistry and Biophysics, 1984
Studies of modification of hemoglobin and of sickle hemoglobin by alternative aspirins have been extended to a series of new bis esters with a variety of substituted bridging diacids and to a group of mono esters with polar acyl groups. Rates of hydrolysis of these alternative aspirins have also been examined, and they reveal that a careful balance ...
E J, Delaney   +3 more
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Crowding and the polymerization of sickle hemoglobin

Journal of Molecular Recognition, 2004
AbstractUnder physiological conditions, sickle hemoglobin, a natural mutant of human hemoglobin A with a surface hydrophobic valine in place of a negatively charged glutamic acid, polymerizes at high volume occupancy. Equilibrium solubility of sickle hemoglobin entails activity coefficients that can approach 103 at high concentrations.
Frank A, Ferrone, Maria A, Rotter
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On the assembly of sickle hemoglobin fascicles

Journal of Molecular Biology, 1989
Deoxyhemoglobin S fibers associate into bundles, or fascicles, that subsequently crystallize by a process of alignment and fusion. We have used electron microscopy to study the formation of fascicles and the changes in fiber packing that occur during the conversion of fascicles to crystals.
W A, McDade   +3 more
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The interactions of sickle hemoglobin

Biochimie, 1972
Resume Les interactions entre molecules d'hemoglobine qui conduisent a la falciformation des erythrocytes, aux crises micro-emboliques et a l'anemie chronique sont dues a la presence de la desoxyhemoglobine S (α 2 a β 2 6Val ). Au cours de la desoxygenation la viscosite des solutions concentrees d'hemoglobine S augmente progressivement; il y a ...
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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   +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   +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   +7 more
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