Effects of Salt Stress on Photosynthetic Pigments and Activity of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase in <Emphasis Type="Italic">Kalidium foliatum</Emphasis>

The effects of NaCl and Na₂SO₄ on photosynthetic pigments, malondialdehyde (MDA), Rubisco activity and superoxide dismutase (SOD) activity were investigated in Kalidium foliatum (Pall.) Moq., which is distributed in the saline soil of Hetao irrigation area in Inner Mongolia China. The K. foliatum plants were treated with NaCl (0, 100, 250, 400 and 500 mM), Na₂SO₄ (0, 100, 250, 400 and 500 mM) and NaCl + Na₂SO₄ (1: 1, v/v) (0, 100, 250, 400 and 500 mM of Na⁺ concentration, 0, 50, 125, 200 and 250 mM of Cl^– and SO ₄ ^2– concentration) for 10 days. Content of chlorophylls and carotenoids were significantly higher than control at increasing NaCl and Na₂SO₄ concentration, in contrast, were significantly reduced by higher concentration of NaCl + Na₂SO₄. Rubisco activity reduced steadily at 100 and 250 mM NaCl, while increased at 400 and 500 mM NaCl. Rubisco activity was significantly higher than control at 100 mM Na₂SO₄, and was no more change under NaCl + Na₂SO₄ treatment. The SOD activity increased with increasing NaCl and Na₂SO₄, and increased at moderate NaCl + Na₂SO₄ treatment. MDA content was lower than control at 250 mM salt concentration. On the basis of the data obtained, K. foliatum showed resistance to salt such as Na⁺, Cl^–and SO ₄ ^2– , Rubisco activity in K. foliatum might be more sensitive to salt.     

转柽柳eIF1A基因烟草的耐盐性分析

目的:验证柽柳eIF1A基因的功能,为通过基因工程手段培育耐盐植物提供基础资料。方法:对转eIF1A基因的烟草和对照烟草进行不同浓度NaCl胁迫实验,测定其相对电导率、SOD活性和丙二醛含量,统计生根率、生长量和盐害程度。结果:转基因烟草的相对电导率、丙二醛含量均随盐浓度的增加而增大,但都较非转基因对照烟草低。SOD活性随着盐浓度的升高而升高,相同浓度NaCl胁迫下各转基因烟草的SOD活性均高于对照烟草的SOD活性。NaCl浓度为240mmol/L时,非转基因对照烟草不能生根,盐害指数高达67.7%;而转基因烟草均能生根,大部分转基因株系的生根率大于50%。结论:柽柳eIF1A基因的转化提高了烟草的耐盐性。     

Proline suppresses Rubisco activity by dissociating small subunits from holoenzyme

Proline caused irreversible inhibition (involving reduction in V(max) without altering K(m) for RuBP) in Rubisco activity. Proline-induced suppression in Rubisco activity did not exceed beyond approximately 65% of the original activity even upon exposure to higher levels of proline for prolonged duration. However, NaCl-induced reduction in Rubisco activity was reversible. Native PAGE analysis of Rubisco-incubated with proline showed the presence of two distinct bands corresponding to approximately 430 and approximately 28 kDa, but that incubated with NaCl showed a single band. SDS-PAGE analysis revealed that the approximately 430- and approximately 28-kDa bands represent octamers of large subunits and dimers of small subunits, respectively. These results demonstrated for the first time that proline suppresses Rubisco activity by bringing about dissociation of the small subunits from the octamer core of large subunits, probably by weakening hydrophobic interactions between them.     

Proline alleviates salt-stress-induced enhancement in ribulose-1, 5-bisphosphate oxygenase activity

Sodium chloride enhanced oxygenase activity while curtailing carboxylase activity of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) purified to electrophoretic homogeneity. Exposure to 200 mM NaCl brought about an increase in the potential of Rubisco to oxygenate RuBP by over 50%. On the other hand, proline suppressed both oxygenase as well as carboxylase activities of Rubisco. Interestingly, proline-induced suppression in oxygenase activity was significantly higher than that of carboxylase activity. Most amazingly, salt-stress-induced enhancement in oxygenase activity was fully alleviated by proline even when present at a concentration as low as 50 mM. The findings presented in this communication clearly demonstrate for the first time that stress-induced proline accumulation might have a critical role in lowering the loss in fixed carbon by curtailing salt-stress-promoted enhancement in oxygenase activity of Rubisco.     

Fruit removal in soybean induces the formation of an insoluble form of ribulose-1,5-bisphosphate carboxylase/oxygenase in leaf extracts*

In some soybean (Glycine max (L.) Merr.) cultivars, fruit removal does not delay the apparent loss of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39) activity and abundance or the decline in photosynthesis. Analysis of leaf extracts from defruited plants indicated a time-dependent increase in both Rubisco activity and abundance in a 30000 · g pellet fraction in cultivars which had been reported to lose all Rubisco protein from the supernatant fraction. Attempts to solubilize the pelleted Rubisco by increasing the buffer volume/tissue ratio or by adding alkylphenoxypolyethoxyethanol (Triton X-100), ethylenediaminetetraacetic acid (EDTA), or NaCl were unsuccessful. However, treatment of the pellets with denaturants such as 8 M urea or 5% (w/v) sodium dodecyl sulfate (SDS) did release Rubisco from the pellet. Redistribution of protein to the pellet fraction appeared to be specific for Rubisco since the amount of ribulose-5-phosphate kinase (EC 2.7.1.19) found in the pellet fraction of leaf extracts of control and defruited plants was small and constant over time. The loss of soluble Rubisco, and the concomitant increase in insoluble Rubisco, in response to fruit removal varied with genotype and was reproducible in both field and greenhouse environments. In addition, the effect was influenced by node position and light; lower and-or shaded leaves exhibited less Rubisco in the pellet fraction than leaves from the top of the plant that was fully exposed to sunlight. When isolated by sucrose-density-gradient centrifugation, the insoluble Rubisco was found to co-purify with a 30-kDa (kilodalton) polypeptide. These results indicate that alteration of the source/sink ratio by removing fruits results in the formation of an insoluble form of Rubisco in leaf extracts of soybean. Whether or not Rubisco exists as an insoluble complex with the 30-kDa polypeptide in intact leaves of defruited plants remains to be determined.Abbreviations kDa kilodalton - PGA kinase 3-phosphoglyceric acid kinase (EC 2.7.2.3) - Rubisco ribulose-1,5-bisphosphate car-boxylase/oxygenase (EC 4.1.1.39) - Ru5P kinase ribulose-5-phosphate kinase (EC 2.7.1.19) - SDS-PAGE sodium dodecyl sulfatepolyacrylamide gel electrophoresis     

Effects of salt stress on growth, photosynthesis and nitrogen fixation in chick-pea (Cicer arietinum L.)

Plants of chick-pea (Cicer arietinum L. cv. ILC1919) inoculated with Mesorhizobium ciceri strain ch-191 were grown in a controlled environmental chamber, and were administered salt (0, 50, 75, and 100 mM NaCl) during the vegetative period. Four harvests (4, 7, 11, and 14d after treatment) were analysed. The aim was to ascertain whether the negative effect of saline stress on nitrogen fixation is due to a limitation on the photosynthate supply to the nodule or a limitation on the nodular metabolism which sustains nitrogenase activity.Plant growth was affected only by the highest NaCl concentration, whereas nitrogenase activity was affected from 50 mM. At the first harvest, Rubisco, PEPC and MDH activities in leaves rose with salt, but fell during the following harvests. The increase of PEPC and MDH in nodules at the two first samplings was clearly related to salt concentration. While 50 mM NaCl increased GS and GOGAT in nodules at some harvests, 100 mM strongly inhibited these activities at all the harvests. The accumulation of proline, amino acids and carbohydrates was clearly related to salt especially in the leaves, whereas in the nodules the protein content was boosted by salt. Although photosynthesis declined with NaCl, the response of nitrogen fixation to salt was more pronounced. This situation, together with carbohydrate accumulation, suggests that the lack of photosynthate does not cause the inhibition of nitrogenase activity under this type of stress. The similar trend observed for the PEPC-MDH pathway and the ARA support the hypothesis concerning the limitation in the supply of energy substrate, mainly malate, to the bacteroids. The accumulation of compatible solutes is more a consequence of damage produced by salt stress than of a protective strategy.     

Ecological studies onTamarix aphylla (L.) Karst

Summary Young saplings ofTamarix aphylla were investigated for their growth intensity under saline irrigation, as well as for the lethal limits of salinity they can tolerate. The saplings were found to be quite sensitive to the addition of NaCl to the irrigation solutions and died when the concentration of the solutions was raised to about 0.7.M NaCl. Growth was depressed even by irrigation with a 0.1M NaCl solution, and no increase in the plant weight was obtained under irrigation with a 0.3M NaCl solution. It, thus, appears thatT. aphylla is not suitable for afforestation of saline habitats.Some aspects of the salt excretion ofT. aphylla were investigated. Sodium and chlorine were found to be excreted most readily and exhibit an optimum type of curve, when the excretion is plotted against the concentration of the irrigation solution. Interrelations between the various ions in the irrigation solutions and the amounts of salts excreted, were found to take place and to parallel the behaviour of these ions in their uptake by the roots. T. aphylla seems to be able to reflect the soil's salinity and the composition of its salts, by the excreted salt crystals.     

Effect of NaCl salinity in vivo and in vitro on ribonuclease activity in the halophyte Suaeda maritima

Ribonuclease (EC 2.7.7.17) activity in the obligate halophyte Suaeda maritima (L.) Dum. var. macrocarpa Moq. was studied in relation to salinity (increasing concentrations of NaCl) of incubation and growth media. In vitro, the addition of 50 to 400 m M NaCl did not affect ribonuclease activity. This result, which was also found for Phaseolus vulgaris , indicates that the hydrolase is insensitive to high saline concentrations. The subcellular distribution of RNase activity did not change significantly with the salinity of the medium or with the age of the plant. The microsomal ribonuclease activity expressed on a fresh weight basis represented in every case less than 6% of the total activity. After 23 days of culture, the absence of salt stimulated the activity of soluble ribonuclease in aerial parts of Suaeda ; inversely, the capacity of the enzyme was lower under optimal saline conditions (130 m M NaCl). This was also evidenced by transfer of whole plants from a non-saline to a saline medium. Such a saline shock caused a decrease followed by a stabilization of the capacity of ribonuclease from Suaeda . The influx of NaCl in the tissues lowered the activity of the hydrolase.     

Possible explanation of the disparity between the in vitro and in vivo measurements of Rubisco activity: a study in loblolly pine grown in elevated pCO2.

Rubisco activity can be measured using gas exchange (in vivo) or using in vitro methods. Commonly in vitro methods yield activities that are less than those obtained in vivo. Rubisco activity was measured both in vivo and in vitro using a spectrophotometric technique in mature Pinus taeda L. (loblolly pine) trees grown using free-air CO2 enrichment in elevated (56 Pa) and current (36 Pa) pCO2. In addition, for studies where both in vivo and in vitro values of Rubisco activity were reported net CO2 uptake rate (A) was modelled based on the in vivo and in vitro values of Rubisco activity reported in the literature. Both the modelling exercise and the experimental data showed that the in vitro values of Rubisco activity were insufficient to account for the observed values of A. A trichloroacetic acid (TCA) precipitation of the protein from samples taken in parallel with those used for activity analysis was co-electrophoresed with the extract used for determining in vitro Rubisco activity. There was significantly more Rubisco present in the TCA precipitated samples, suggesting that the underestimation of Rubisco activity in vitro was attributable to an insufficient extraction of Rubisco protein prior to activity analysis. Correction of in vitro values to account for the under-represented Rubisco yielded mechanistically valid values for Rubisco activity. However, despite the low absolute values for Rubisco activity determined in vitro, the trends reported with CO2 treatment concurred with, and were of equal magnitude to, those observed in Rubisco activity measured in vivo.     

Heat Denaturation Profiles of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco) and Rubisco Activase and the Inability of Rubisco Activase to Restore Activity of Heat-Denatured Rubisco

We compared the heat-denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase and further examined the ability of Rubisco activase to restore the activity of heat-denatured Rubisco originally reported (E. Sanchez de Jimenez, L. Medrano, and E. Martinez-Barajas [1995] Biochemistry 34: 2826-2831). Rubisco was heat-treated in both the carbamylated and uncarbamylated forms and in the presence and absence of 10 mM dithiothreitol (DTT). Both forms were highly resistant to heat denaturation and further protection was gained in the presence of DTT. A 50% loss in total activity occurred after 1 h at 57.5 and 55.2[deg]C for uncarbamylated Rubisco and at 60.2 and 59.6[deg]C for carbamylated Rubisco, in each case with and without DTT, respectively. In contrast, Rubisco activase lost 50% activity after only 5 min at 33[deg]C and the loss in activity was not affected by the presence of Rubisco. When Rubisco, heat-denatured to various extents, was incubated at room temperature with Rubisco activase or bovine serum albumin as a control, Rubisco activase did not have a significant specific ability to restore Rubisco activity. We conclude that Rubisco activase alone does not have the ability to restore the activity of heat-denatured Rubisco and is unlikely to protect or restore Rubisco activity from heat denaturation in vivo because it is more heat-labile than Rubisco.     

The absence of Rubisco activase activity in total wheat leaf extracts is recovered in the purified protein

When desalted extracts of soluble protein from dark-adaptedwheat leaves were assayed for ribulose-1, 5-bisphosphate carboxylase/oxygenase(Rubisco) activase activity in the presence of 1 mM ATP andan ATP-regenerating system, very little ATP-dependent activationof RuBP-inactivated Rubisco was found. In extracts from light-adaptedleaves a very similar pattern of Rubisco activation was observedexcept that the overall level of Rubisco activity was much lowerthan in the extracts from dark-adapted leaves. These featureswere apparent both at low (120µg per ml) and high (640µg per ml) protein concentrations. We were unable to demonstrateRubisco activase activity in crude leaf extracts. Consequently,in order to establish that Rubisco activase was present in wheatleaf extracts the wheat leaf protein was purified to homogeneity.The identity of the protein was confirmed with antibodies tothe spinach enzyme, ATPase activity and activase-mediated releaseof the inhibitor, carboxyara-binitol-1-phosphate (CA1P) fromthe tertiary Rubisco complex. The pure wheat Rubisco activaserelieved the CA1P-induced inhibition of Rubisco activity. Rubiscoactivase had no significant effect on the affinity of wheatRubisco for the substrate, ribulose-1, 5-bisphosphate (RuBP). Key words: Rubisco activase, Rubisco, regulation     

Programmed cell death in salt glands of <Emphasis Type="Italic">Tamarix aphylla</Emphasis> L.: an electron microscope analysis

Background  

Tamarix aphylla is a halophyte growing in soils rich in NaCl. Leaves of Tamarix aphylla develop numerous salt glands, which initiate, secrete NaCl, become senescent and eventually die, as part of a programmed process. Dead glands are replaced by new ones, so that only active glands exist on the leaves. Most importantly, these glands remove excess NaCl from the tissues, which protects against hyperosmotic phenomena.     

Development and testing of a novel lab-scale direct steam-injection apparatus to hydrolyse model and saline crop slurries

In this work, a novel laboratory-scale direct steam-injection apparatus (DSIA) was developed to overcome the main drawback of the conventional batch-driven lab rigs, namely the long time needed to heat fiber slurry from room to reaction temperatures greater than 150 °C. The novel apparatus mainly consisted of three units: (i) a mechanically-stirred bioreactor where saturated steam at 5-30 bar can be injected; (ii) an automatic on-off valve to flash suddenly the reaction medium after a prefixed reaction time; (iii) a cyclone separator to recover the reacted slurry. This system was tested using 0.75 dm3 of an aqueous solution of H?SO? (0.5%, v/v) enriched with 50 kg m?3 of either commercial particles of Avicel? and Larch xylan or 0.5 mm sieved particles of Tamarix jordanis. Each slurry was heated to about 200 °C by injecting steam at 28 bar for 90 s. The process efficiency was assessed by comparing the dissolution degree of suspended solid (Y(S)), as well as xylose (Y(X)), glucose (Y(G)), and furfural (Y(F)) yields, with those obtained in a conventional steam autoclave at 130 °C for 30 or 60 min. Treatment of T. jordanis particles in DSIA resulted in Y(S) and Y(G) values quite similar to those obtained in the steam autoclave at 130 °C for 60 min, but in a less efficient hemicellulose solubilization. A limited occurrence of pentose degradation products was observed in both equipments, suggesting that hydrolysis predominated over degradation reactions. The susceptibility of the residual solid fractions from DSIA treatment to a conventional 120 h long cellulolytic treatment using an enzyme loading of 5.4 FPU g?1 was markedly higher than that of samples hydrolysed in the steam autoclave, their corresponding glucose yields being equal to 0.94 and 0.22 g per gram of initial cellulose, respectively. Thus, T. jordanis resulted to be a valuable source of sugars for bioethanol production as proved by preliminary tests in the novel lab rig developed here.     

Cysteines 449 and 459 modulate the reduction-oxidation conformational changes of ribulose 1.5-bisphosphate carboxylase/oxygenase and the translocation of the enzyme to membranes during stress

The role of cysteines 449 (Cys449) and 459 (Cys459) from the large subunit (LS) of ribulose 1-5-bisphosphate carboxylase/oxygenase (Rubisco) in the reduction-oxidation (redox) regulation of the enzyme was assessed by site-directed mutagenesis of these residues and chloroplast transformation of Chlamydomonas reinhardtii. In vitro studies indicated that mutations C449S, C459S or C449S/ C459S do not affect the activity and proteolytic susceptibility of the enzyme in the reduced state. However, when oxidized, the mutant enzymes differed from the wild type (WT), showing an increased resistance to inactivation and, in the case of the double mutant (DM), an altered structural conformation as reflected by the kinetics of proteolysis with subtilisin. The response of the DM strain to saline stress revealed that the absence of Cys449 and Cys459 intensifies Rubisco degradation and the covalent disulfide and non-disulfide polymerization of the enzyme in vivo. Saline stress also induced Rubisco translocation to a membrane (M) fraction that contained only covalently polymerized enzyme. Rubisco mobilization to this M fraction was enhanced also in the DM strain. Altogether, these results indicate that Cys449 and Cys459 participate in the modulation of the conformational changes promoted by oxidative modifications retarding processes related to the catabolism of the enzyme in vivo.     

Wide-Area Estimates of Stand Structure and Water Use of Tamarix spp. on the Lower Colorado River: Implications for Restoration and Water Management Projects

Tamarix spp. removal has been proposed to salvage water and allow native vegetation to recolonize western U.S. riparian corridors. We conducted wide‐area studies on the Lower Colorado River to answer some of the scientific questions about Tamarix water use and the consequences of removal, combining ground surveys with remote sensing methods. Tamarix stands had moderate rates of evapotranspiration (ET), based on remote sensing estimates, averaging 1.1 m/yr, similar to rates determined for other locations on the river and other rivers. Leaf area index values were also moderate, and stands were relatively open, with areas of bare soil interspersed within stands. At three Tamarix sites in the Cibola National Wildlife Refuge, groundwater salinity at the site nearest to the river (200 m) was relatively low (circa 2,250 mg/L) and was within 3 m of the surface. However, 750 and 1,500 m from the river, the groundwater salinity was 5,000–10,000 mg/L due to removal of water by the Tamarix stands. Despite the high groundwater salinity, the sites away from the river did not have saline surface soils. Only 1% of the mean annual river flow is lost to Tamarix ET on the Lower Colorado River in the United States, and the opportunities for water salvage through Tamarix removal are constrained by its modest ET rates. A possible alternative to Tamarix removal is to intersperse native plants among the stands to improve the habitat value of the riparian zone.     

Malic dehydrogenase from tamarix roots: effects of sodium chloride in vivo and in vitro

Soluble and mitochondrial malic dehydrogenases (MDH) were isolated from root tips of the halophyte Tamarix tetragyna L. grown in the presence and absence of NaCl. The activity of the enzymes isolated from root tips grown in the presence of NaCl was lower than that of the enzymes isolated from roots grown in absence of NaCl. The mitochondrial MDH was much more sensitive to salinity than the soluble MDH. The soluble enzyme from roots grown in NaCl had a higher Km for malate and lower Km for NAD than enzyme from the control roots. Addition of NaCl in vitro at 72 mM significantly stimulated the reductive activity of soluble MDH, while higher NaCl concentrations (240 mM and above) depressed enzyme activity. The inhibition of enzyme activity by various salts was found to be in the order MgCl₂ > NaCl = KCl > Na₂SO₄. Mannitol at equiosmotic concentrations had no effect. Substrate inhibition, typical for oxaloacetate oxidation, was not observed at high NaCl concentrations in vitro and high substrate concentrations neutralized the inhibitory effect of NaCl. Increased coenzyme concentrations had no effect. In vitro NaCl increased the Km for malate and oxaloacetate already at relatively low concentrations. At the same time NaCl decreased the Km for NAD and NADH. The inhibitory effect of NaCl on enzyme activity seems not to be due to the effect on the Km alone. Soluble and mitochondrial MDH had different responses to pH changes, mitochondrial MDH being more sensitive. Mitochondrial MDH released from the particles had a similar response to that of the entire particles. Changes of pH modified the effect of NaCl on enzyme activity. It was postulated that NaCl apparently induces conformational changes in the enzyme.     

Rubisco活化酶的研究进展

Rubisco活化酶是近年中发现的一种可以调节Rubisco活性的酶 ,它能使Rubisco在植株体内条件下达到最大活化程度。Rubisco活化酶不仅具有活化Rubisco的活性 ,而且具有ATP水解酶活性。在ATP水解过程中 ,Rubisco活化酶促使各种磷酸糖抑制物从Rubisco上解离下来 ,恢复Rubisco活性。Rubisco活化酶的发现与研究使许多Rubisco体内活化中的疑难问题得到了阐明。本文还介绍了Rubisco活化酶的分子特性、酶作用机制以及环境因素对它活性影响等方面的最新研究进展。     

The effects of salinity on photosynthesis and growth of the single-cell C<Subscript>4</Subscript> species <Emphasis Type="Italic">Bienertia sinuspersici</Emphasis> (Chenopodiaceae)

Recent research on the photosynthetic mechanisms of plant species in the Chenopodiaceae family revealed that three species, including Bienertia sinuspersici, can carry out C₄ photosynthesis within individual photosynthetic cells, through the development of two cytoplasmic domains having dimorphic chloroplasts. These unusual single-cell C₄ species grow in semi-arid saline conditions and have semi-terete succulent leaves. The effects of salinity on growth and photosynthesis of B. sinuspersici were studied. The results show that NaCl is not required for development of the single-cell C₄ system. There is a large enhancement of growth in culture with 50–200 mM NaCl, while there is severe inhibition at 400 mM NaCl. With increasing salinity, the carbon isotope values (δ¹³C) of leaves increased from −17.3^o/_oo (C₄-like) without NaCl to −14.6^o/_oo (C₄) with 200 mM NaCl, possibly due to increased capture of CO₂ from the C₄ cycle by Rubisco and reduced leakiness. Compared to growth without NaCl, leaves of plants grown under saline conditions were much larger (~2 fold) and more succulent, and the leaf solute levels increased up to ~2000 mmol kg solvent⁻¹. Photosynthesis on an incident leaf area basis (CO₂ saturated rates, and carboxylation efficiency under limiting CO₂) and stomatal conductance declined with increasing salinity. On a leaf area basis, there was some decline in Rubisco content with increasing salinity up to 200 mM NaCl, but there was a marked increase in the levels of pyruvate, Pi dikinase, and phosphoenolpyruvate carboxylase (possibly in response to sensitivity of these enzymes and C₄ cycle function to increasing salinity). The decline in photosynthesis on a leaf area basis was compensated for on a per leaf basis, up to 200 mM NaCl, by the increase in leaf size. The influence of salinity on plant development and the C₄ system in Bienertia is discussed.     

Rubisco活化酶的研究进展

Rubisco活化酶是近年中发现的一种可以调节Rubisco活性的酶,它能使Rubisco在植株体内条件下达到最大活化程度。Rubisco活化酶不仅具有活化Rubisco的活性,而且具有ATP水解酶活性。在ATP水解过程中,Rubisco活化酶促使各种磷酸糖抑制物从Rubisco上解离下来,恢复Rubisco活性。Rubisco活化酶的发现与研究使许多Rubisco体内活化中的疑难问题得到了阐明。本文还介绍了Rubisco活化酶的分子特性、酶作用机制以及环境因素对它活性影响等方面的最新研究进展。     

Sea fennel (<Emphasis Type="Italic">Crithmum maritimum</Emphasis> L.) under salinity conditions: a comparison of leaf and root antioxidant responses

The present study was carried out to compare the effect of NaCl on growth, cell membrane damage, and antioxidant defences in the halophyte Crithmum maritimum L. (sea fennel). Physiological and biochemical changes were investigated under control (0 mM NaCl) and saline conditions (100 and 300 mM NaCl). Biomass and growth of roots were more sensitive to NaCl than leaves. Roots were distinguished from leaves by increased electrolyte leakage and high malondialdehyde (MDA) concentration. Superoxide dismutase (SOD), catalase (CAT) and ascorbate peroxidase (APX) activities, ascorbic acid (AA) and glutathione (GSH) concentrations were lower in the roots than in the leaves of control plants. The different activity patterns of antioxidant enzymes in response to 100 and 300 mM NaCl indicated that leaves and roots reacted differently to salt stress. Leaf CAT, APX and glutathione reductase (GR) activities were lowest at 300 mM NaCl, but they were unaffected by 100 mM NaCl. Only SOD activity was reduced in the latter treatment. Root SOD activity was significantly decreased in response to 300 mM NaCl and root APX activity was significantly higher in plants treated with 100 and 300 mM compared to the controls. The other activities in roots were insensitive to salt. The concentration of AA decreased in leaves at 100 and 300 mM NaCl, and in roots at 300 mM NaCl, when compared to control plants. The concentrations of GSH in NaCl-treated leaves and roots were not significantly different from the controls. In both organs, AA and GSH were predominating in the total pool in ascorbic acid and glutathione, under control or saline conditions.