Skip to main content
PMC home page
Biophysical Journal logoLink to Biophysical Journal
. 1981 Jan;33(1):63–79. doi: 10.1016/S0006-3495(81)84872-2

Diffusion coefficients of hemoglobin by intensity fluctuation spectroscopy: effects of varying pH and ionic strength.

K J LaGattuta, V S Sharma, D F Nicoli, B K Kothari
PMCID: PMC1327397  PMID: 7272438

Abstract

Measurements of the mutual diffusion coefficients (D) of the liganded human hemoglobins (Hb) oxy-HbA and oxy-HbS were performed as a function of Hb concentration (CHb), pH, and ionic strength (tau) by intensity fluctuation spectroscopy (IFS). Average diffusion coefficients, (D), and normalized variances, ((D/(D) - 1)2), were recorded. Results are reported and select features are discussed quantitatively. (a) for tau = 0.15 M, the shape of the (d) vs. CHb curve is found to vary with pH. We developed a precise description of this effect in the form of an algebraic relationship between (D), CHb, and Z, the titration charge. (b) only slight differences between the (D) values of oxy-HbS and oxy-HbA are observed, at tau = 0.15 M, for CHb Less Than or Equal To 10 g%. These differences are explained by the theory of part a. (c) No evidence of aggregation is found in solutions of oxy-HbA or oxy-HbS, at tau = 0.15 M, for CHb Less Than or Equal To 10 g%. (d) Indications of aggregation appear in oxy-HbA solutions at very low concentrations of salt. An estimate is made of the extent of aggregation, and the average radius of a cluster is determined.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alpert S. S., Banks G. The concentration dependence of the hemoglobin mutual diffusion coefficient. Biophys Chem. 1976 May;4(3):287–296. doi: 10.1016/0301-4622(76)80077-4. [DOI] [PubMed] [Google Scholar]
  2. Elbaum D., Nagel R. L., Herskovits T. T. Aggregation of deoxyhemoglobin S at low concentrations. J Biol Chem. 1976 Dec 10;251(23):7657–7660. [PubMed] [Google Scholar]
  3. Girling R. L., Schmidt W. C., Jr, Houston T. E., Amma E. L., Huisman T. H. Molecular packing and intermolecular contacts of sickling deer type III hemoglobin. J Mol Biol. 1979 Jul 5;131(3):417–433. doi: 10.1016/0022-2836(79)90001-9. [DOI] [PubMed] [Google Scholar]
  4. Jones C. R., Johnson C. S., Jr Photon correlation spectroscopy of hemoglobin: diffusion of oxy-HbA and oxy-HbS. Biopolymers. 1978 Jun;17(6):1581–1593. doi: 10.1002/bip.1978.360170615. [DOI] [PubMed] [Google Scholar]
  5. Keller K. H., Canales E. R., Yum S. I. Tracer and mutual diffusion coefficients of proteins. J Phys Chem. 1971 Feb 4;75(3):379–387. doi: 10.1021/j100673a015. [DOI] [PubMed] [Google Scholar]
  6. Lindstrom T. R., Koenig S. H., Boussios T., Bertles J. F. Intermolecular interactions of oxygenated sickle hemoglobin molecules in cells and cell-free solutions. Biophys J. 1976 Jun;16(6):679–689. doi: 10.1016/S0006-3495(76)85721-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Magdoff-Fairchild B., Chiu C. C. X-ray diffraction studies of fibers and crystals of deoxygenated sickle cell hemoglobin. Proc Natl Acad Sci U S A. 1979 Jan;76(1):223–226. doi: 10.1073/pnas.76.1.223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Nagel R. L., Bookchin R. M., Johnson J., Labie D., Wajcman H., Isaac-Sodeye W. A., Honig G. R., Schilirò G., Crookston J. H., Matsutomo K. Structural bases of the inhibitory effects of hemoglobin F and hemoglobin A2 on the polymerization of hemoglobin S. Proc Natl Acad Sci U S A. 1979 Feb;76(2):670–672. doi: 10.1073/pnas.76.2.670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. PAULING L., ITANO H. A. Sickle cell anemia a molecular disease. Science. 1949 Nov 25;110(2865):543–548. doi: 10.1126/science.110.2865.543. [DOI] [PubMed] [Google Scholar]
  10. Raj T., Flygare W. H. Diffusion studies of bovine serum albumin by quasielastic light scattering. Biochemistry. 1974 Jul 30;13(16):3336–3340. doi: 10.1021/bi00713a024. [DOI] [PubMed] [Google Scholar]
  11. Williams R. C., Jr Concerted formation of the gel of hemoglobin S. Proc Natl Acad Sci U S A. 1973 May;70(5):1506–1508. doi: 10.1073/pnas.70.5.1506. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Wilson W. W., Luzzana M. R., Penniston J. T., Johnson C. S., Jr Pregelation aggregation of sickle cell hemoglobin. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1260–1263. doi: 10.1073/pnas.71.4.1260. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. von Casimir W., Kaiser N., Keilmann F., Mayer A., Vogel H. Dielectric properties of oxyhemoglobin and deoxyhemoglobin in aqueous solution at microwave frequencies. Biopolymers. 1968;6(12):1705–1715. doi: 10.1002/bip.1968.360061205. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES