Effect of Sodium Chloride on Expansion Rates and Invertase Activity of Leaves

1978 ◽  
Vol 5 (1) ◽  
pp. 73 ◽  
Author(s):  
JS Hawker ◽  
RR Walker

The rate of expansion and the invertase (�-fructofuranosidase, EC 3.2.1.26) activity of leaves of two relatively salt-sensitive plants, Phaseolus vulgaris and Zea mays, decreased with increasing concentrations of NaCl from 0 to 50 mM in nutrient solutions supplied regularly in a porous growth medium. Sucrose concentrations in the leaves were higher and reducing sugar concentrations were lower at the higher concentrations of NaCl. Growth of leaves, invertase activity, and concentrations of reducing sugar and sucrose changed much less, if at all, with NaCl treatment of Hordeum vulgare, a reasonably salt-tolerant plant. Cellulase activities were not different in bean leaves from plants grown on different NaCl concentrations. The Km values for sucrose for invertase from bean leaves were 5.8, 8.1 and 10.4 mM for plants grown on 0, 20 and 50 mM NaCl respectively. NaCl at concentrations up to 200 mM did not affect the in vitro activity of invertase from barley, bean or maize leaves.


1996 ◽  
Vol 23 (1) ◽  
pp. 25 ◽  
Author(s):  
Y Gao ◽  
KC Woo

The effects of metabolites, protein phosphorylation and malate inhibition on phosphoenolpyruvate carboxylase (PEPC) activity were investigated at pH 7.0 in partially purified enzyme from maize leaves. Glycine, glucose 6-phosphate or alanine stimulated the activity two- to three-fold. Glycine and glucose 6-phosphate increased the affinity for PEP by factors of eight and four respectively. These metabolites changed the response of the enzyme activity to pH. Activity increased between pH 6.8 and 8.0 by 10-fold in the absence and 26% in the presence of these metabolites. In vitro phosphorylation of PEPC increased the activity two-fold in the absence but not in the presence of these metabolites. Malate was a strong inhibitor of PEPC, the KI value being 0.25-0.5 mM. Protein phosphorylation and the above metabolites increased the Ki value by factors of three and 12 respectively, but they synergistically increased the Ki 50-fold, thus providing maximal protection against malate inhibition. In the crude extracts from light- and dark-adapted leaves in the presence of a physiological concentration of malate (20 mM), PEPC activity comparable to the photosynthetic rate was obtained only from the light-adapted leaves in the presence of metabolites indicating that both light-induced protein phosphorylation and metabolic activators were essential for PEPC activation during photosynthesis. We propose that both these factors act synergistically to modulate PEPC during photosynthesis in maize.



Planta Medica ◽  
2012 ◽  
Vol 78 (05) ◽  
Author(s):  
A Husni ◽  
S Ross ◽  
O Dale ◽  
C Gemelli ◽  
G Ma ◽  
...  


Planta Medica ◽  
2014 ◽  
Vol 80 (16) ◽  
Author(s):  
JB Althaus ◽  
G Jerz ◽  
P Winterhalter ◽  
M Kaiser ◽  
R Brun ◽  
...  


Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
P Sartorelli ◽  
ML Yoshinaga ◽  
MJP Ferreira ◽  
JHG Lago ◽  
LFD Passero




2019 ◽  
Author(s):  
G Vanti ◽  
V Dourdouni ◽  
D Lazari ◽  
C Panagiotidis ◽  
SG Ntallis ◽  
...  




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