@article{cd75ae74af53454d9d9d40a996a4a2b8,
title = "Measurement of the translation mobility of concanavalin a in glycerol-saline solutions and on the cell surface by fluorescence recovery after photobleaching",
abstract = "The fluorescence recovery kinetics of succinyl-fluorescein Concanavalin A (S-F-ConA) in glycerol-physiological saline solutions of high viscosity and when bound to the surface of mouse fibroblast were measured following brief photobleaching using a laser excited fluorescence microscope. In the high viscosity solutions, the recovery kinetics, interpreted on the basis of a simple diffusion model, yielded a diffusion coefficient in close agreement with the values predicted by the Stokes-Einstein equation. Recovery kinetics for S-F-ConA bound to the surface of mouse 3T3 and SV3T3 cells cultured in vitro yielded diffusion coefficients in the range of 5-10·10-11 cm2/s, values considerably lower than those reported previously for membrane protiens. These measurement indicated that a considerable fraction of the S-F-ConA molecules bound to the cell surface are immobilized. These results are discussed in relation to current concepts of lateral motion of protein components within natural membranes.",
author = "K. Jacobson and E. Wu and G. Poste",
note = "Funding Information: the mobility of ConA-receptor complexes within the membrane \[3,5,6,14\]. The possibility also exists that the high concentration of sulfated glycosaminoglycans associated with the outer face of the plasma membrane could further restrict the lateral diffusion of ConA-receptor complexes and other molecules within the membrane (see refs. 2, 15). Consequently, the lateral mobility of certain classes of plasma membrane components cannot be considered solely in terms of their ability to diffuse within a lipid bilayer and other membrane components together with membrane-associated structures could exert significant effects on their translational mobility. Indeed, such additional restraints may be of considerable importance in maintaining the spatial organization and topographic distribution of different classes of molecules on the cell surface (see refs. 3,5,6,14,16). The present observation that the recovery of S-F-ConA fluorescence in bleached areas of the cell surface is never 100% provides further evidence to support the above proposal that a certain fraction of ConA-receptor complexes may be immobilized within the plasma membrane, though the nature of the surface components responsible for restriction of lateral diffusion in the present system remains to be identified. Two other recent photobleaching studies of ConA mobility on a variety of cultured cells have yielded qualitatively similar results \[1 7,18\]. We thank H. Allen and research colleagues in membrane biophysics in the Department of Applied Physics and Chemistry at Cornell University for many helpful discussions and we also acknowledge Y. Hou, M.E. Conroy, A. MacKearnin, and J. Morey for their excellent technical assistance, and K. Paigen for the use of the fluorescence microscope. This work was supported by Grant No. CA-16743 (K.J.) and CA-13393 (G.P.) from the National Institutes of Health. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",
year = "1976",
month = apr,
day = "16",
doi = "10.1016/0005-2736(76)90189-9",
language = "English (US)",
volume = "433",
pages = "215--222",
journal = "BBA - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "1",
}