Proton-transport activity, sidedness, and morphometry of tonoplast and plasma-membrane vesicles purified by free-flow electrophoresis from roots of Lepidium sativum L. and hypocotyls of Cucurbita pepo L.

Planta ◽  
1992 ◽  
Vol 186 (4) ◽  
pp. 483-494 ◽  
Author(s):  
Günther F. E. Scherer ◽  
Barbara vom Dorp ◽  
Claudia Schöllmann ◽  
Dieter Volkmann
1988 ◽  
Vol 86 (2) ◽  
pp. 631-637 ◽  
Author(s):  
Hervé Canut ◽  
Andrew Brightman ◽  
Alain M. Boudet ◽  
D. James Morré

Planta ◽  
1991 ◽  
Vol 184 (4) ◽  
Author(s):  
Herv� Canut ◽  
Sylvie Baudracco ◽  
Mireille Caban� ◽  
Alain-Michel Boudet ◽  
G�rard Marigo

1990 ◽  
Vol 271 (2) ◽  
pp. 297-303 ◽  
Author(s):  
E Pola ◽  
J Bertran ◽  
A Roca ◽  
M Palacín ◽  
A Zorzano ◽  
...  

1. In the present study we have examined the sensitivity of A and ASC amino-acid-carrier activities in rat liver plasma-membrane vesicles to the thiol-group modifying reagents N-ethylmaleimide (NEM) and iodoacetamide (IA). To this end, the different Na(+)-dependent entities involved in alanine transport were assessed. 2. NEM inactivated Na(+)-dependent alanine transport as a result of the inhibition of both system A and ASC transport activities. The functional sensitivity of system A to NEM was greater than that of system ASC. 3. The presence of L-alanine (10 mM) during the exposure of vesicles to NEM afforded partial protection to system A, but not to the ASC, carrier. This effect was specific, since the presence of L-phenylalanine (10 mM) did not cause any protection. 4. Na+ did not protect A or ASC carriers against NEM inactivation; however, the presence of Na+ (100 mM-NaCl) and L-alanine (10 mM) during the exposure of the vesicles to NEM protected against inactivation of system A and ASC transport activities. The extent of protection was greater in the case of the system ASC transport activity than in the case of the A carrier. 5. IA also diminished Na(+)-dependent alanine transport by inhibition of A and ASC transport activities. Sodium and L-alanine afforded protection to both A and ASC transport activities from the inhibitory action of IA. The extent of protection induced by substrates was similar for both carriers. 6. It is concluded that there is one, or several, free thiol groups in A and ASC carriers, the integrity of which is essential for transport activity. Sensitivity to thiol-group-specific reagents and the pattern of protection with substrates against inactivation is different in A and ASC carriers. That suggests the existence of topological dissimilarities regarding the thiol-group containing site(s) in A and ASC amino acid carriers.


2016 ◽  
Vol 15 (3) ◽  
pp. 900-913 ◽  
Author(s):  
Roberto de Michele ◽  
Heather E. McFarlane ◽  
Harriet T. Parsons ◽  
Miranda J. Meents ◽  
Jeemeng Lao ◽  
...  

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