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Literature DB >> 264675

Ligand kinetics of hemoglobin S containing erythrocytes.

J P Harrington, D Elbaum, R M Bookchin, J B Wittenberg, R L Nagel.

Abstract

Oxygen uptake of fully deoxygenated sickle (SS) erythrocytes is slower than that of normal (AA) erythrocytes, as demonstrated by the half-times of the overall oxygenation reactions: at 25 degrees in an isotonic phosphate buffer the normal red cells have a t1/2 = 82 +/- 4.7 msec, as compared to sickle red cells where t1/2 = 135 +/- 17.6 msec. The effects of temperature, extracellular osmolality, and the presence of an antisickling agent (n-butylurea) on the rate of red cell oxygenation strongly suggest that the differences in oxygenation rates encountered with sickle red cells is directly related to the intracellular polymerization of deoxyhemoglobin S.

Entities: Chemical Gene

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Year: 1977 PMID： 264675 PMCID： PMC393226 DOI： 10.1073/pnas.74.1.203

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

17 in total

1. Oxygen dissociation curves in sickle cell anemia and in subjects with the sickle cell trait.

Authors: M R BECKLAKE; S B GRIFFITHS; M McGREGOR; H I GOLDMAN; J P SCHREVE
Journal: J Clin Invest Date: 1955-05 Impact factor: 14.808

2. Stopped-flow measurements of CO and O2 uptake by hemoglobin in sheep erythrocytes.

Authors: J A SIRS; F J ROUGHTON
Journal: J Appl Physiol Date: 1963-01 Impact factor: 3.531

3. Photocolorimetric determination of rate of uptake of CO and O2 by reduced human red cell suspensions at 37 degrees C.

Authors: R E FORSTER; F J ROUGHTON; F KREUZER; W A BRISCOE
Journal: J Appl Physiol Date: 1957-09 Impact factor: 3.531

4. Titratable sulfhydryl groups of normal and sickle cell hemoglobins at O degrees and 38 degrees.

Authors: M MURAYAMA
Journal: J Biol Chem Date: 1957-09 Impact factor: 5.157

5. Studies on the destruction of red blood cells. XII. Factors influencing the role of S hemoglobin in the pathologic physiology of sickle cell anemia and related disorders.

Authors: M S GREENBERG; E H KASS; W B CASTLE
Journal: J Clin Invest Date: 1957-06 Impact factor: 14.808

6. The kinetics of human haemoglobin in solution and in the red cell at 37 degrees C.

Authors: Q H GIBSON; F KREUZER; E MEDA; F J ROUGHTON
Journal: J Physiol Date: 1955-07-28 Impact factor: 5.182

7. The rate of distribution of dissolved gases between the red blood corpuscle and its fluid environment: Part I. Preliminary experiments on the rate of uptake of oxygen and carbon monoxide by sheep's corpuscles.

Authors: H Hartridge; F J Roughton
Journal: J Physiol Date: 1927-01-12 Impact factor: 5.182

8. Some observations on the kinetics of haemoglobin in solution and in the haemoglobin in solution and in the red blood corpuscle.

Authors: J W LEGGE; F J W ROUGHTON
Journal: Biochem J Date: 1950 Jun-Jul Impact factor: 3.857

9. Studies on abnormal hemoglobins. I. Their demonstration in sickle cell anemia and other hematologic disorders by means of alkali denaturation.

Authors: K SINGER; A I CHERNOFF; L SINGER
Journal: Blood Date: 1951-05 Impact factor: 22.113

Ligand kinetics of hemoglobin S containing erythrocytes.

1. Oxygen dissociation curves in sickle cell anemia and in subjects with the sickle cell trait.

2. Stopped-flow measurements of CO and O2 uptake by hemoglobin in sheep erythrocytes.

3. Photocolorimetric determination of rate of uptake of CO and O2 by reduced human red cell suspensions at 37 degrees C.

4. Titratable sulfhydryl groups of normal and sickle cell hemoglobins at O degrees and 38 degrees.

5. Studies on the destruction of red blood cells. XII. Factors influencing the role of S hemoglobin in the pathologic physiology of sickle cell anemia and related disorders.

6. The kinetics of human haemoglobin in solution and in the red cell at 37 degrees C.

7. The rate of distribution of dissolved gases between the red blood corpuscle and its fluid environment: Part I. Preliminary experiments on the rate of uptake of oxygen and carbon monoxide by sheep's corpuscles.

8. Some observations on the kinetics of haemoglobin in solution and in the haemoglobin in solution and in the red blood corpuscle.

9. Studies on abnormal hemoglobins. I. Their demonstration in sickle cell anemia and other hematologic disorders by means of alkali denaturation.

10. Blood oxygen dissociation curves in sickle cell disease.

1. Fiber depolymerization: fracture, fragments, vanishing times, and stochastics in sickle hemoglobin.

2. Sickle hemoglobin polymer melting in high concentration phosphate buffer.

3. An analysis of the stopped-flow kinetics of gaseous ligand uptake and release by adult mouse erythrocytes.

4. Kinetics of increased deformability of deoxygenated sickle cells upon oxygenation.

5. The influence of deformation of transformed erythrocytes during flow on the rate of oxygen release.

6. Molecular and cellular pathogenesis of hemoglobin SC disease.

7. Alternative aspirins as antisickling agents: acetyl-3,5-dibromosalicylic acid.