Literature DB >> 3790684

Quasi-elastic laser light scattering from solutions and gels of hemoglobin S.

Z Kam, J Hofrichter.   

Abstract

Quasi-elastic light scattering has been used to examine solutions and gels of deoxyhemoglobin S. The autocorrelation function is found to decay with a characteristic exponential relaxation which can be ascribed to the diffusion of monomer (64,000 molecular weight) hemoglobin S molecules. In the absence of polymers, the relaxation time is in good agreement with previous measurements of the diffusion coefficient for solutions of normal human hemoglobin. In the presence of the polymer phase, a large (greater than 200-fold) increase in the scattered intensity is observed but no contribution to the decay of the autocorrelation function from the motion of the aligned polymer phase can be detected. Heterodyning between the time-independent scattering amplitude from the polymers and the time-dependent scattering of the diffusing monomers results in a twofold increase in the relaxation time arising from monomer diffusion.

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Year:  1986        PMID: 3790684      PMCID: PMC1329828          DOI: 10.1016/S0006-3495(86)83544-5

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  16 in total

1.  Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution.

Authors:  B C Wishner; K B Ward; E E Lattman; W E Love
Journal:  J Mol Biol       Date:  1975-10-15       Impact factor: 5.469

2.  Gelation of sickle cell hemoglobin in mixtures with normal adult and fetal hemoglobins.

Authors:  H R Sunshine; J Hofrichter; W A Eaton
Journal:  J Mol Biol       Date:  1979-10-09       Impact factor: 5.469

3.  Kinetics of sickle hemoglobin polymerization. III. Nucleation rates determined from stochastic fluctuations in polymerization progress curves.

Authors:  J Hofrichter
Journal:  J Mol Biol       Date:  1986-06-05       Impact factor: 5.469

4.  Structure of hemoglobin S fibers: optical determination of the molecular orientation in sickled erythrocytes.

Authors:  J Hofrichter; D G Hendricker; W A Eaton
Journal:  Proc Natl Acad Sci U S A       Date:  1973-12       Impact factor: 11.205

5.  A thermodynamic model for gelation of sickle-cell hemoglobin.

Authors:  A P Minton
Journal:  J Mol Biol       Date:  1974-02-05       Impact factor: 5.469

6.  Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques.

Authors:  F A Ferrone; J Hofrichter; W A Eaton
Journal:  J Mol Biol       Date:  1985-06-25       Impact factor: 5.469

7.  Hemoglobin aggregation in single red blood cells of sickle cell anemia.

Authors:  I Nishio; T Tanaka; S T Sun; Y Imanishi; S T Ohnishi
Journal:  Science       Date:  1983-06-10       Impact factor: 47.728

8.  Molecular topology in crystals and fibers of hemoglobin S.

Authors:  S J Edelstein
Journal:  J Mol Biol       Date:  1981-08-25       Impact factor: 5.469

9.  Oxygen binding by sickle cell hemoglobin polymers.

Authors:  H R Sunshine; J Hofrichter; F A Ferrone; W A Eaton
Journal:  J Mol Biol       Date:  1982-06-25       Impact factor: 5.469

10.  Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism.

Authors:  F A Ferrone; J Hofrichter; W A Eaton
Journal:  J Mol Biol       Date:  1985-06-25       Impact factor: 5.469

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  8 in total

1.  Intermolecular interactions, nucleation, and thermodynamics of crystallization of hemoglobin C.

Authors:  Peter G Vekilov; Angela R Feeling-Taylor; Dimiter N Petsev; Oleg Galkin; Ronald L Nagel; Rhoda Elison Hirsch
Journal:  Biophys J       Date:  2002-08       Impact factor: 4.033

2.  Monomer diffusion and polymer alignment in domains of sickle hemoglobin.

Authors:  M R Cho; F A Ferrone
Journal:  Biophys J       Date:  1992-07       Impact factor: 4.033

3.  Aggregation of normal and sickle hemoglobin in high concentration phosphate buffer.

Authors:  Kejing Chen; Samir K Ballas; Roy R Hantgan; Daniel B Kim-Shapiro
Journal:  Biophys J       Date:  2004-10-01       Impact factor: 4.033

4.  Theoretical description of the spatial dependence of sickle hemoglobin polymerization.

Authors:  H X Zhou; F A Ferrone
Journal:  Biophys J       Date:  1990-09       Impact factor: 4.033

5.  Calculations of scattered light from rigid polymers by Shifrin and Rayleigh-Debye approximations.

Authors:  M F Bishop
Journal:  Biophys J       Date:  1989-11       Impact factor: 4.033

6.  Monomer diffusion into polymer domains in sickle hemoglobin.

Authors:  M R Cho; F A Ferrone
Journal:  Biophys J       Date:  1990-10       Impact factor: 4.033

7.  A study of the dynamic properties of the human red blood cell membrane using quasi-elastic light-scattering spectroscopy.

Authors:  R B Tishler; F D Carlson
Journal:  Biophys J       Date:  1993-12       Impact factor: 4.033

Review 8.  The polymerization of sickle hemoglobin in solutions and cells.

Authors:  F A Ferrone
Journal:  Experientia       Date:  1993-02-15
  8 in total

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