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Concanavalin A binds to the endoplasmic reticulum and the starch grain surface of root statocytes.

Authors :
Schneider, E.
Sievers, Andreas
Source :
Planta: An International Journal of Plant Biology; 1981, Vol. 152 Issue 3, p177-180, 4p
Publication Year :
1981

Abstract

Using Concanavalin A (Con A) labeled with fluorescein isothiocyanate, we studied the intracellular localization of receptor molecules in the calyptra of 24-h dark-grown cress roots. Fixation in glutaraldehyde gave positive binding of the distal complex of the endoplasmic reticulum and the nucelus in the statocytes. In contrast, fixation in formaldehyde did not preserve the membrane-associated receptors, but revealed Con A affinity of the starch grain surface within the amyloplasts. Treatment of glutaraldehydefixed sections with non-ionic detergents led to partial solubilization of membrane components: the starch grain surface turned positive, though the positive binding of Con A to the endoplasmic reticulum and the nucleus remained unaffected. We therefore conclude that the Con A receptor in the membrane is a glycoprotein tightly inserted in other components of the compartment. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00320935
Volume :
152
Issue :
3
Database :
Complementary Index
Journal :
Planta: An International Journal of Plant Biology
Publication Type :
Academic Journal
Accession number :
70760576
Full Text :
https://doi.org/10.1007/BF00385141