𝔖 Bobbio Scriptorium
✦   LIBER   ✦

A computer-controlled microfluorometer with laser illumination: Study of lectin interaction with surfaces of human erythrocytes

✍ Scribed by X. Albe; M.-A. Deugnier; M. Caron; J.-C. Bisconte


Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
751 KB
Volume
15
Category
Article
ISSN
0010-4809

No coin nor oath required. For personal study only.

✦ Synopsis


A fluorescence microscope based on a laser illumination and controlled by a computer is described. The instrumentation, its connection with the computer, and the developed FOR-TRAN programs are detailed. This semiautomatic system is easy to use and allows a cell-bycell analysis of undisturbed cultured cells or of cell suspensions. An application to the study of fluorescent lectin interaction with plasma membranes of human erythrocytes is reported. For each sample the mean values and/or the distribution patterns of the detected fluorescence intensities are calculated or plotted. Thus, binding kinetics are obtained, showing that quantitation of site densities using a constant illuminated area is a valuable approach of the ligand-receptor interaction. The possibilities offered by a software extension are also mentioned.


πŸ“œ SIMILAR VOLUMES


Interactions of lectins with CHO cell su
✍ D. Emerson; R. L. Juliano πŸ“‚ Article πŸ“… 1982 πŸ› John Wiley and Sons 🌐 English βš– 768 KB

## Abstract The binding of radioiodinated lectins to the CHO cell surface was measured for the following affinity purified plant agglutinins; concanavalin A, wheat germ agglutinin, Ricinus agglutinins (I, II), pea agglutinin, peanut agglutinin, and __Bandeiria simpliciafolia__ agglutinin (BSLI). Th

Distribution of glycophorin on the surfa
✍ Gahmberg, Carl G. ;TaurΓ©n, Georg ;Virtanen, Ismo ;Wartiovaara, Jorma πŸ“‚ Article πŸ“… 1978 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 901 KB

## Abstract Human erythrocyte membranes of the En(a–) blood group lack the major sialoglycoprotein (glycophorin). By absorption of a crude antiglycophorin antiserum with En(a–) membranes a specific antiglycophorin antiserum was obtained. By immune electron microscopy we showed that glycophorin is r