Abstract
Studies of red blood cells (RBCs) and RBC ghosts, using a quasi-elastic light scattering (QELS) microscope spectrometer, have identified the membrane as the primary source of the light scattering signal. This is the first report in which motion of the cell membrane has been demonstrated to be the primary source of the QELS signal from a cell. Cytoplasmic changes induced in the RBC by varying the osmotic strength of the medium were also detected using this technique. Comparison of the data from white blood cells (WBCs) with the RBC data demonstrated significant differences between different types of cells.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Carlson F. D., Fraser A. B. Dynamics of F-actin and F-actin complexes. J Mol Biol. 1974 Oct 25;89(2):273–281. doi: 10.1016/0022-2836(74)90518-x. [DOI] [PubMed] [Google Scholar]
- Coletta M., Hofrichter J., Ferrone F. A., Eaton W. A. Kinetics of sickle haemoglobin polymerization in single red cells. Nature. 1982 Nov 11;300(5888):194–197. doi: 10.1038/300194a0. [DOI] [PubMed] [Google Scholar]
- Englert D. F. An optical study of isolated rat adrenal chromaffin cells. Exp Cell Res. 1980 Feb;125(2):369–376. doi: 10.1016/0014-4827(80)90131-7. [DOI] [PubMed] [Google Scholar]
- Haskell R. C., Carlson F. D. Quasi-elastic light-scattering studies of single skeletal muscle fibers. Biophys J. 1981 Jan;33(1):39–62. doi: 10.1016/S0006-3495(81)84871-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Lin S., Snyder C. E., Jr High affinity cytochalasin B binding to red cell membrane proteins which are unrelated to sugar transport. J Biol Chem. 1977 Aug 10;252(15):5464–5471. [PubMed] [Google Scholar]
- MCCONAGHEY P. D., MAIZELS M. The osmotic coefficients of haemoglobin in red cells under varying conditions. J Physiol. 1961 Jan;155:28–45. doi: 10.1113/jphysiol.1961.sp006611. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Muirhead H., Cox J. M., Mazzarella L., Perutz M. F. Structure and function of haemoglobin. 3. A three-dimensional fourier synthesis of human deoxyhaemoglobin at 5.5 Angstrom resolution. J Mol Biol. 1967 Aug 28;28(1):117–156. doi: 10.1016/s0022-2836(67)80082-2. [DOI] [PubMed] [Google Scholar]
- Mustacich R. V., Ware B. R. A study of protoplasmic streaming in Nitella by laser Doppler spectroscopy. Biophys J. 1976 May;16(5):373–388. doi: 10.1016/S0006-3495(76)85695-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nishio I., Peetermans J., Tanaka T. Microscope laser light scattering spectroscopy of single biological cells. Cell Biophys. 1985 Jun;7(2):91–105. doi: 10.1007/BF02784485. [DOI] [PubMed] [Google Scholar]
- Nishio I., Tanaka T., Sun S. T., Imanishi Y., Ohnishi S. T. Hemoglobin aggregation in single red blood cells of sickle cell anemia. Science. 1983 Jun 10;220(4602):1173–1175. doi: 10.1126/science.6857241. [DOI] [PubMed] [Google Scholar]
- Schindler M., Koppel D. E., Sheetz M. P. Modulation of membrane protein lateral mobility by polyphosphates and polyamines. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1457–1461. doi: 10.1073/pnas.77.3.1457. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sun S. T., Tanaka T., Nishio I., Peetermans J., Maizel J. V., Jr, Piatigorsky J. Direct observation of delta-crystallin accumulation by laser light-scattering spectroscopy in the chicken embryo lens. Proc Natl Acad Sci U S A. 1984 Feb;81(3):785–787. doi: 10.1073/pnas.81.3.785. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sung K. L., Schmid-Schönbein G. W., Skalak R., Schuessler G. B., Usami S., Chien S. Influence of physicochemical factors on rheology of human neutrophils. Biophys J. 1982 Jul;39(1):101–106. doi: 10.1016/S0006-3495(82)84495-0. [DOI] [PMC free article] [PubMed] [Google Scholar]