Electrorotation of lymphocytes—The influence of membrane events and nucleus

1986 ◽  
Vol 6 (11) ◽  
pp. 973-982 ◽  
Author(s):  
Heiko Ziervogel ◽  
Roland Glaser ◽  
Dieter Schadow ◽  
Stephan Heymann
Keyword(s):  
Electrical Properties ◽  
Cell Membrane ◽  
Electric Fields ◽  
Concanavalin A ◽  
High Frequency ◽  
Human Peripheral Blood ◽  
Peripheral Blood Lymphocytes ◽  
Cell Interior ◽  
Membrane Conductivity ◽  
Human Peripheral Blood Lymphocytes

Electrorotation—the spin of cells in rotating high frequency electric fields—has been used to investigate properties of human peripheral blood lymphocytes. The rotation spectra of lymphocytes deviate from those of single shell spheres. The deviations are caused by the electrical properties of the nucleus in the cell interior. Electrorotation allows the distinction between successfully stimulated lymphocytes and unstimulated cells after application of concanavalin A. Notwithstanding the fact that only a proportion of the cells will be mitogenically stimulated we detected an enhanced cell membrane conductivity for the whole cell population immediately after the addition of mitogen.

scholarly journals Flow cytometric analysis of lectin binding to human peripheral blood lymphocytes

1982 ◽  
Vol 208 (1) ◽  
pp. 69-75 ◽  
Author(s):  
G Blackledge ◽  
B Vose ◽  
A J Morris ◽  
D Crowther ◽  
J T Gallagher
Keyword(s):  
Concanavalin A ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Lectin Binding ◽  
Surface Membrane ◽  
Flow Cytometric Analysis ◽  
Peripheral Blood Lymphocytes ◽  
Blood Lymphocytes ◽  
Human Peripheral Blood Lymphocytes ◽  
Lentil Lectin

The binding of fluorescein-conjugated lentil lectin and concanavalin A to the surface membrane of human peripheral blood lymphocytes was studied by flow cytometry. The lymphocytes bound 3-fold more lentil lectin molecules compared with concanavalin A molecules and lentil lectin binding approached saturation at a much lower concentration than did that of concanavalin A. Lentil lectin identified two groups of lymphocytes: a low-binding T-cell fraction and a high-binding B-cell-enriched fraction. Concanavalin A did not discriminate between these populations in unseparated lymphocytes. Competition studies indicated that lentil lectin and concanavalin A were bound to different sites on the lymphocyte surface, although about 50% of lentil lectin sites were in close proximity to concanavalin A sites.

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