Effect of High Sodium Chloride Concentrations in the Growth Medium on the Activity of Glucose-6-Phosphate Dehydrogenase From Pea Roots

1974 ◽  
Vol 1 (4) ◽  
pp. 483 ◽  
Author(s):  
A Poljakoff-Mayber ◽  
H Greenway

The experiments reported in this paper examined discrepant results, obtained in earlier investigations, concerning the effects of NaCl in the growth medium of vascular plants on the specific activity of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) extracted from the plants. NaCl at 120 mM or higher concentrations increased the specific activity of the enzyme in extracts from roots of germinating peas. However, this effect of NaCl was only clearly expressed when 0.1M phosphate was the buffer used to extract the enzyme. When organic buffers were used the observed increase in enzyme activity was either much smaller or absent. Increases in specific activity of glucose-6-phosphate dehydrogenase were only found in extracts from roots that showed severely retarded growth and some brown discoloration. No increase in activity was found either when 120 mM NaCl was added to the growth medium after seedling establishment, or if seeds were germinated in 75 mM NaCl. These observations account for the discrepancies reported in the literature.

2003 ◽  
Vol 34 ◽  
pp. 128-130 ◽  
Author(s):  
Ana Paula L. Delamare ◽  
Thais Dalcin ◽  
Gabriela Müller ◽  
Sergio Olavo Pinto da Costa ◽  
Sergio Echeverrigaray

1975 ◽  
Vol 148 (2) ◽  
pp. 259-268 ◽  
Author(s):  
M Orlowski ◽  
M Goldman

The specific activity and total activity of glucose 6-phosphate dehydrogenase (EC 1.1.1.49) under conditions of complete cell breakage fall 10-20-fold during a 3h period of spore germination and outgrowth. The spores must germinate (lose refractility), but do not have to undergo outgrowth, for the loss of activity to occur. Glucose 6-phosphate dehydrogenase activity from cells as any stage of development is completely stable in extracts at 4 degrees C or 30 degrees C. All of the enzyme activity is found in a soluble (50000g supernatant) fraction and remains completely soluble throughout development. Soluble protein and total cellular protein remain constant for about 2h. Proteinases could not be detected or protein turnover demonstrated during the morphogenetic process. Phenylmethanesuophony fluoride and o-phenanthroline, inhibitors of proteolytic enzymes, do not prevent glucose 6-phosphate dehydrogenase inactivation when added to whole cells. Mixing experiments show no inhibitor of glucose 6-phosphate dehydrogenase to be present in late-stage cells. The enzyme is not excreted into the culture medium. Chloramphenicol and rifampicine immediately stop protein synthesis and development but not the inactivation of glucose 6-phosphate dehydrogenase. NaN3, 2,4-dinitrophenol or anaerobiosis immediately stop development and prevent the loss of enzyme activity. A requirement for metabolic energy is therefore probable. Extracts of spores pre-labelled with L[14C]leucine were made at various stages of morphogenesis and subjected to polyacrylamide-gel electrophoresis. Glucose 6-phosphate dehydrogenase, which was identified by a specific stain, did not lose 14C label, and therefore may not be degraded during the inactivation process.


1971 ◽  
Vol 49 (8) ◽  
pp. 953-958 ◽  
Author(s):  
E. L. Pugh ◽  
M. K. Wassef ◽  
M. Kates

A cell-free enzyme preparation from Halobacterium cutirubrum was shown to catalyze the biosynthesis of fatty acids from malonyl-CoA at zero sodium chloride concentration, with a specific activity about [Formula: see text] that of a similarly prepared fatty acid synthetase from E. coli. Both the H. cutirubrum synthetase and that from E. coli were strongly inhibited by high sodium chloride or potassium chloride concentrations (0.5–4 M). The malonyl-CoA: ACP transacylase, which catalyzes the first step in the fatty acid biosynthetic pathway, was shown to be strongly inhibited by salt in H. cutirubrum, but not in E. coli. It is concluded that H. cutirubrum contains a fatty acid synthetase system which normally operates at a very low level of activity as a result of inhibition by the high intracellular salt concentration present in this organism.


1979 ◽  
Vol 57 (5) ◽  
pp. 396-401 ◽  
Author(s):  
Hsiao-Lin Chang ◽  
Darold Holten ◽  
Rom Karin

The distribution of the multiple molecular forms of rat liver and mammary gland glucose-6-phosphate dehydrogenase was determined by electrophoresis on 5% polyacrylamide gels. In both of these organs, changes in the distribution of enzyme activity among the several forms was slight even when approximately 20- to 40-fold changes in enzyme specific activity were achieved by fasting-refeeding experiments (for liver) or during pregnancy and lactation (for mammary gland), it was concluded that the induction of glucose-6-phosphate dehydrogenase in these two organs occurs without any major redistribution among the multiple molecular forms of this enzyme.


Sign in / Sign up

Export Citation Format

Share Document