NaCl胁迫对棉花种子萌发和幼苗生长的伤害

采用盐化土壤盆栽方法,选择耐盐性较强品种枝棉３号和耐盐性较弱品种泗棉２号,研究了盐分对棉花（Ｇｏｓｓｙｐｉｕｍ ｈｉｒｓｕｔｕｍ Ｌ．）种子萌发、出苗和幼苗生长的伤害。结果表明,在－０．５５和－１．１０ＭＰａ盐分胁迫下,对棉花伤害起决定性作用的因子是Ｎａ＾＋。２００ｍｍｏｌ／Ｌ ＮａＣｌ胁迫下,枝棉３号种子萌发时电导率上升幅度和子叶ＣＡＴ下降幅度均显著小于泗棉２号。１００和２００ｍｍｏｌ／Ｌ Ｎａ     

NaCl胁迫下棉花体内 Na~+ 、K~+分布与耐盐性

采用盐化土壤方法 ,选择苗期耐盐性较强的陆地棉品种枝棉 3号和中棉所 1 9及耐盐性较弱的品种泗棉 2号和苏棉 1 2号 ,研究了盐胁迫下棉苗体内 Na+、K+的运输和分配与耐盐性的关系。结果表明 ,耐盐品种根系具有一定的截留 Na+作用。棉花地上部盐分器官水平上的区域化分布特征明显 :2 0 0 mmol/L Na Cl胁迫下 ,枝棉 3号叶片中的 Na+含量显著低于泗棉 2号 ,茎及叶柄中的 Na+含量显著高于泗棉 2号 ;棉株地上部茎、叶柄、叶片中的 Na+含量分别由下而上逐渐减小 ,相同节位的茎、叶柄中的 Na+含量大于叶片 ,枝棉 3号更显著。1 0 0 mmol/L和 1 50 mmol/L Na Cl胁迫下 ,枝棉 3号和中棉所 1 9K+/Na+显著高于泗棉 2号和苏棉 1 2号。Na+在茎和叶柄中滞留和积累 ,根中的 K+向地上部选择性运输 ,以维持叶片中较高的 K+/Na+,是棉花耐盐性的一个重要特点     

NaCl胁迫下抗盐突变体和野生型小麦Na^2＋,K^＋累积的差异分析

对抗盐突变体和野生型小麦在盐胁迫下Ｎａ＾＋、Ｋ＾＋的累积状况进行了比较研究。结果表明，ＮａＣｌ胁迫下突变体根和叶中Ｎａ＾＋的相对累积较野生型显著地少，同时Ｎａ＾＋的净累积速率显著地低。这种Ｎａ＾＋相对累积少的状况在叶中表现尤为明显。两者叶中Ｋ＾＋含量随盐浓度的增加显著下降，但突变体的含量均高于野生型。突变体根中Ｋ＾＋的含量也显著高于野生型，且这种差异随盐度的提高而增大。分别统计突变体和野生型根和叶     

盐分胁迫条件下甜菜碱对小麦幼苗体内Na^＋,K^＋和Cl^—的含量及 …

以抗盐品种茶淀红和盐敏感品种中国春等两种小麦为实验材料,研究甜菜碱对盐分胁迫条件下小麦幼苗Ｎａ＾＋、Ｋ＾＋、Ｃｌ＾－的吸收、分配的影响。结果表明：外源甜菜碱能够在一定程度上限制幼苗对Ｎａ＾＋、Ｋ＾＋、Ｃｌ＾－的吸收、分配的影响。结果表明：外源甜菜碱能够在一定程度上限制幼苗对Ｎａ＾＋、Ｃｌ＾－的吸收,阻滞其向地上部分运输的数量和速度,同时提高体内Ｋ＾＋含量、向上运输效率,降低地上部分对Ｎａ＾＋、Ｋ＾     

盐胁迫下无花果细胞质和液泡膜H^＋—ATPase活性对脯氨酸积累 …

盐胁迫降低无花果振荡培养细胞培养液ＰＨ添加质膜Ｈ＾＋－ＡＴＰａｓｅ活性抑制剂Ｎａ３ＶＯ４则抑制盐诱导的培养液ＰＨ下降,表明盐诱导培养液Ｈ下降主要是细胞质膜Ｈ＾＋－ＡＴＰａｓｅ活性增加的结果。ＮａＣｌ处理提高活体细胞质膜Ｈ＾＋－ＡＴＰａｓｅ活性,而降低膜微囊Ｈ＾＋－ＡＴＰａｓｅ活性,培养液中添加Ｎａ３ＶＯ４ ５０μｍｏｌ／Ｌ完全抑制盐胁迫下无花果细胞游离脯氨酸只累,但添加更高浓度Ｎａ３ＶＯ４,则提高     

NaCl胁迫番茄苗的生长和营养元素积累（简报）

在ＮａＣｌ胁迫下番茄植株生长速率和营养元素积累均下降,但两品种的花冠比没有改变。不同品种番茄植株的生长和根冠部元素的积累对ＮａＣｌ胁迫的响应在异。１００ｍｏｌ·Ｌ＾－１ＮａＣｌ处理下,Ｋ＾＋积累与植株生长速率呈显著正相关,Ｃａ＾２＋、Ｍｇ＾２＋的积累与生长速率相关性不显著。     

NaCl胁迫对小麦抗盐突变体根液包膜H^＋—ATP酶和H^＋—PP酶活性的影响

随着盐胁迫强度（ＮａＣｌ０～１５０ｍｍｏｌ／Ｌ）和时间（０～７２ｈ）的增加,小麦抗盐突变体根液泡膜Ｈ＾＋－ＡＴＰ酶和Ｈ＾＋－ＰＰ酶活性显著增加,虽然野生型酶活性在盐胁迫下也有增加,但其增加的幅度显著低于突变体,Ｈ＾＋－ＰＰ酶活性的差异更为显著。Ｈ＾＋－ＡＴＰ酶和Ｈ＾＋－ＰＰ酶的最适ｐＨ值在两者之间以及盐胁迫前后均无改变,分别为７．０和８．０。无盐胁迫下野生型液胞泡５８ｋＤ蛋白带缺失,盐胁迫下这一蛋     

CO2倍增环境生长的小麦幼苗对盐胁迫的生理反应

研究了ＣＯ２倍增／盐胁迫对不同抗盐性冬小麦幼苗有机干重,Ｋ＾＋,Ｎａ＾＋,Ｃａ＾＋＋,Ｍｇ＾＋＋含量,脯氨酸水平及蛋白质变化的效应,表明两种小麦生长在１５０ｍｍｏｌ／ＬＮａＣｌ下,其有机干重,Ｋ＾＋,Ｃａ＾＋＋,Ｍｇ＾＋＋含量下降,而Ｎａ＾＋明显长高;ＣＯ２倍增可增加小麦有机干重,使一价阳离子Ｋ＾＋,Ｎａ＾＋含量升高,二价阳离子Ｃａ＾＋＋,Ｍｇ＾＋＋呈下降趋势,同时有利于游离脯氨酸的积累,并为植物     

NaCl胁迫下抗盐突变体和野生型小麦Na~ 、K~ 累积的差异分析

对抗盐突变体和野生型小麦（ＴｒｉｔｉｃｕｍａｅｓｔｉｖｕｍＬ．）在盐胁迫下Ｎａ＋、Ｋ＋的累积状况进行了比较研究。结果表明,ＮａＣｌ胁迫下突变体根和叶中Ｎａ＋的相对累积较野生型显著地少,同时Ｎａ＋的净累积速率显著地低。这种Ｎａ＋相对累积少的状况在叶中表现尤为明显。两者叶中Ｋ＋含量随盐浓度的增加显著下降,但突变体的含量均高于野生型。突变体根中Ｋ＋的含量也显著高于野生型,且这种差异随盐浓度的提高而增大。分别统计突变体和野生型根和叶中Ｎａ＋的含量以及每株幼苗的Ｎａ＋总量以分析二者Ｎａ＋在根和叶中的分布差异,结果表明３００ｍｍｏｌ／ＬＮａＣｌ胁迫９６ｈ后,突变体根中Ｎａ＋的累积量占其整株幼苗Ｎａ＋累积总量的４４４％,而野生型根中含量占其总量的２４３％。相对于野生型而言,在盐胁迫下突变体根中Ｎａ＋分布比例的提高可有效地减少根中Ｎａ＋向地上部分转运。     

水稻高脯氨酸愈伤组织变异体的选择及其耐盐性

以水稻（ＯｒｙｚａｓａｔｉｖａＬ．）品种双丰１号幼胚愈伤组织为材料,经５０ＣＯγ－射线诱变处理后,用羟基脯氨酸（Ｈｙｐ）作为选择压力,通过多次在含Ｈｙｐ（３．０ｍｍｏｌ／Ｌ）的选择培养基和无Ｈｙｐ培养基上交替培养,分离出耐Ｈｙｐ的愈伤组织变异体。该变异体以高脯氨酸含量为特征,其脯氨酸含量比原型高２．６倍;在ＮａＣｌ处理时,随着ＮａＣｌ浓度的提高,变异体愈伤组织脯氨酸含量的增加大大高于原型。这种高脯氨酸变异体的耐盐性较原型强,用相对鲜重估计其耐性比对照提高３９％。变异体在盐胁迫下可溶性糖含量比原型多,吸收较多的Ｎａ＋,并维持较高的Ｋ＋含量;但Ｋ＋／Ｎａ＋比与原型无差异。变异体含水量略有下降。这些性状的变化显示了变异体在盐胁迫下渗透调节的加强。     

Kinetic studies on the (Na+ + K+)-dependent ATPase. Evidence for coexisting sites for Na+, K+ and Mg2+

Na⁺-ATPase activity of a dog kidney (Na⁺ + K⁺)-ATPase enzyme preparation was inhibited by a high concentration of NaCl (100 mM) in the presence of 30 μM ATP and 50 μM MgCl₂, but stimulated by 100 mM NaCl in the presence of 30 μM ATP and 3 mM MgCl₂. The $\text{K}{}_{0.5}$ for the effect of MgCl₂ was near 0.5 mM. Treatment of the enzyme with the organic mercurial thimerosal had little effect on Na⁺-ATPase activity with 10 mM NaCl but lessened inhibition by 100 mM NaCl in the presence of 50 μM MgCl₂. Similar thimerosal treatment reduced (Na⁺ + K⁺)-ATPase activity by half but did not appreciably affect the $\text{K}{}_{0.5}$ for activation by either Na⁺ or K⁺, although it reduced inhibition by high Na⁺ concentrations. These data are interpreted in terms of two classes of extracellularly-available low-affinity sites for Na⁺: Na⁺-discharge sites at which Na⁺-binding can drive E₂-P back to E₁-P, thereby inhibiting Na⁺-ATPase activity, and sites activating E₂-P hydrolysis and thereby stimulating Na⁺-ATPase activity, corresponding to the K⁺-acceptance sites. Since these two classes of sites cannot be identical, the data favor co-existing Na⁺-discharge and K⁺-acceptance sites. Mg²⁺ may stimulate Na⁺-ATPase activity by favoring E₂-P over E₁-P, through occupying intracellular sites distinct from the phosphorylation site or Na⁺-acceptance sites, perhaps at a coexisting low-affinity substrate site. Among other effects, thimerosal treatment appears to stimulate the Na⁺-ATPase reaction and lessen Na⁺-inhibition of the (Na⁺ + K⁺)-ATPase reaction by increasing the efficacy of Na⁺ in activating E₂-P hydrolysis.     

Mechanisms by which Li+ stimulates the (Na++K+)-dependent ATPase

The addition of LiCl stimulated the (Na⁺+K⁺)-dependent ATPase activity of a rat brain enzyme preparation. Stimulation was greatest in high Na⁺/low K⁺ media and at low Mg. ATP concentrations. Apparent affinities for Li⁺ were estimated at the α-sites (moderate-affinity sites for K⁺ demonstrable in terms of activation of the associated K⁺-dependent phosphatase reaction), at the β-sites (high-affinity sites for K⁺ demonstrable in terms of activation of the overall ATPase reaction), and at the Na⁺ sites for activation. The relative efficacy of Li⁺ was estimated in terms of the apparent maximal velocity of the phosphatase and ATPase reactions when Li⁺ was substituted for K⁺, and also in terms of the relative effect of Li⁺ on the apparent K_M for Mg· ATP. With these data, and previously determined values for the apparent affinities of K⁺ and Na⁺ at these same sites, quantitative kinetic models for the stimulation were examined. A composite model is required in which Li⁺ stimulates by relieving inhibition due to K⁺ and Na⁺ (i) by competing with K⁺ for the α-sites on the enzyme through which K⁺ decreases the apparent affinity for Mg·ATP and (ii) by competing with Na⁺ at low-affinity inhibitory sites, which may represent the external sites at which Na⁺ is discharged by the membrane NA⁺/K⁺ pump that this enzyme represents. Both these sites of action for Li⁺ would thus lie, in vivo, on the cell exterior.     

Relative roles of Ca2+, Sr2+, Ba2+ and Mg2+ in controlling lens permeability characteristics

The effects of barium, strontium and magnesium upon lens permeability characteristics were studied in the presence and absence of 2 mM calcium in the bathing medium. Permeability characteristics were determined by measuring lens potential, resistance and ⁴²K efflux rates. Barium and strontium at equimolar concentrations to calcium were able to substitute for calcium in controlling lens sodium permeability. Magnesium was ineffective in this respect.Small changes in resistance and ⁴²K efflux rates occurred when calcium was eliminated from bathing solution containing either 2 mM barium or strontium. These changes were interpreted to be the result of an increase in lens permeability to potassium. When 2 mM strontium was added to calcium-containing solution, there was no significant change in the electrical or flux parameters of the lens. However, the addition of 2 mM barium to calcium-containing solution resulted in a 54% increase in lens resistance and a 13 mV depolarization. These observations indicated a barium-induced decrease in lens permeability to potassium, and this was confirmed by an observed decrease in ⁴²K efflux rate constant under similar experimental conditions.The rapid time course of all the observed changes implies that they are the result of changes in the permeability characteristics of membranes lying close to the surface of the lens.     

A reconstituted Na++K+ pump in liposomes containing purified (Na++K+-ATPase from kidney medulla

Liposomes containing either purified or microsomal (Na⁺,K⁺)-ATPase preparations from lamb kidney medulla catalyzed ATP-dependent transport of Na⁺ and K⁺ with a ratio of approximately 3Na⁺ to 2K⁺, which was inhibited by ouabain. Similar results were obtained with liposomes containing a partially purified (Na⁺,K⁺-ATPase from cardiac muscle. This contrasts with an earlier report by Goldin and Tong (J. Biol. Chem. 249, 5907–5915, 1974), in which liposomes containing purified dog kidney (Na⁺,K⁺)-ATPase did not transport K⁺ but catalyzed ATP-dependent symport of Na⁺ and Cl^?. When purified by our procedure, dog kidney (Na⁺,K⁺)-ATPase showed some ability to transport K⁺ but the ratio of Na⁺ : K⁺ was 5 : 1.     

Effects of interrupted K+ supply on growth and uptake of K+, Ca2+, Mg2+ and Na+ in spring wheat

Effects of interrupted K⁺ supply on different parameters of growth and mineral cation nutrition were evaluated for spring wheat (Triticum aestivum L. cv. Svenno). K⁺ (2.0 mM) was supplied to the plants during different periods in an otherwise complete nutrient solution. Shoot growth was reduced before root growth after interruption in K⁺ supply. Root structure was greatly affected by the length of the period in K⁺ -free nutrient solution. Root length was minimal, and root branching was maximal within a narrow range of K⁺ status of the roots. This range corresponded to cultivation for the last 1 to 3 days, of 11 in total, in K⁺ -free nutrient solution, or to continuous cultivation in solution containing 0.5 to 2 mM K⁺. In comparison, both higher and lower internal/external K⁺ concentrations had inhibitory effects on root branching. However, the differing root morphology probably had no significant influence on the magnitude of Ca²⁺, Mg²⁺ and Na⁺ uptake. Uptake of Ca²⁺ and especially Mg²⁺ significantly increased after K⁺ interruption, while Na⁺ uptake was constant in the roots and slowly increased in the shoots. The two divalent cations could replace K⁺ in the cells and maintain electroneutrality down to a certain minimal range of K⁺ concentrations. This range was significantly higher in the shoot [110 to 140 μmol (g fresh weight)^?1] than in the root [20 to 30 μmol (g fresh weight)^?1]. It is suggested that the critical K⁺ values are a measure of the minimal amount of K⁺ that must be present for physiological activity in the cells. At the critical levels, K⁺ (⁸⁶Rb) influx and Ca²⁺ and Mg²⁺ concentrations were maximal. Below the critical K⁺ values, growth was reduced, and Ca²⁺ and Mg²⁺ could no longer substitute for K⁺ for electrostatic balance. In a short-term experiment, the ability of Ca²⁺ to compete with K⁺ in maintaining electroneutrality in the cells was studied in wheat seedlings with different K⁺ status. The results indicate that K⁺, which was taken up actively and fastest at the external K⁺ concentration used (2.0 mM), partly determines the size of Ca²⁺ influx.     

Effect of calmodulin,Ca2+ and Mg2+ on the (Ca2+ + Mg2+)-ATPase of erythrocyte membranes

Calmodulin-depleted isotonic erythrocyte ghosts contain 200 ng residual calmodulin/mg protein which is not removed by extensive washings at pCa²⁺ > 7. Specific activity and Ca²⁺-affinity of the (Ca²⁺ + Mg²⁺)ATPase increase at increasing calmodulin, with K_{0.5 Ca} of 0.38 μM at calmodulin concentrations corresponding to that in erythrocytes. High Ca²⁺ concentrations inhibit the enzyme. Specific activity and Ca²⁺-affinity of the enzyme decrease at increasing Mg²⁺ concentrations. The Ca²⁺ ? Mg²⁺ antagonism is likewise observed at inhibitory Ca²⁺ concentrations.     

Gel electrophoretic identity of the (Na+ + Mg2+)- and (Na+ + Ca2+)-stimulated phosphorylations of rat brain ATPase

The classical E₂-P intermediate of (Na⁺ + K⁺)-ATPase dephosphorylates readily in the presence of K⁺ and is not affected by the addition of ADP. To determine the significane in the reaction cycle of (Na⁺ + K⁺)-ATPase of kinetically atypical phosphorylations of rat brain (Na⁺ + K⁺)-ATPase we compared these phosphorylated components with the classical E₂-P intermediate of this enzyme by gel electrophoresis. When rat brain (Na⁺ + K⁺)-ATPase was phosphorylated in the presence of high concentrations of Na⁺ a proportion of the phosphorylated material formed was sensitive to ADP but resistant to K⁺. Similarly, if phosphorylation was carried out in the presence of Na⁺ and Ca²⁺ up to 300 pmol/mg protein of a K⁺-resistant, ADP-sensitive material were formed. If phosphorylation was from [γ-³²P]CTP up to 800 pmol ³²P/mg protein of an ADP-resistant, K⁺-sensitive phosphorylated matterial were formed. On gel electrophoresis these phosphorylated materials co-migrated with authentic Na⁺-stimulated, K⁺-sensitive, E₂-P-phosphorylated intermediate of (Na⁺ + K⁺)-ATPase, supporting suggestions that they represent phosphorylated intermediates in the reaction sequence of this enzyme.     

Binding of Cd2+, Ni2+, Cu2+ and Zn2+ by isolated envelopes of Pseudomonas fluorescens

Abstract Cell envelopes of Pseudomonas fluorescens , cytoplasmic membrane, peptidoglycan and outer membrane were obtained from a fractionation procedure and tested for their metal binding capacity. Isolated envelopes (cytoplasmic membrane, peptidoglycan and outer membrane) were chemically modified and functional carboxyl groups transformed to electropositive amine groups, using carbodiimide ethylenediamine. Transformation of carboxyl groups was evaluated by measuring total amine groups in all fractions (modified or not). Using equilibrium dialysis and Scatchard plots for the data, we have established that isolated unmodified cell envelopes (cytoplasmic membrane, peptidoglycan and outer membrane) possess at least two types of metal binding sites with different association constants ( K _a and K '_a). Introduction of positive charges into the bacterial envelopes resulted in the disappearance of one type of metal binding site which had the highest association constant value for Ni²⁺, Cu²⁺ and Zn²⁺. All fractions, modified or not, always presented at least two types of binding sites with different association constants for Cd²⁺.     

Synthetic peptide K+ carrier with Ca2+ inhibition

Based on a proposed solution conformation of the Ca²⁺ ion complex of the repeat hexapeptide of elastin, l-Val-l-Ala-l-Pro-Gly-l-Val-Gly, it is possible to modify the molecule making it more lipophilic for lipid bilayer permeation while retaining its complexation features. Therefore the two peptides, For-MeVal-Ala-Pro-Sar-Pro-Sar-OMe and For-MeVal-Ala-Pro-Sar-Pro-Sar-OH, were synthesized and evaluated for lipid bilayer activity and cation binding (For, N-formyl; Me, N-methyl; Sar, N-methyl glycine). Both peptides bound Ca²⁺ preferentially but did not exhibit the properties of a Ca²⁺ carrier. They were however active as K⁺ carriers although K⁺ ion titration curves showed a much lower affinity for K⁺ than for Ca²⁺. The addition of Ca²⁺ or Mg²⁺ to the bilayer system inhibited the peptide K⁺ carrier activity. Three possible explanations of this interesting Ca²⁺ inhibition of carrier activity are irreversible complexation of Ca²⁺, mixed ligand complex formation involving Ca²⁺, lipid and peptide, and impermeability of the lipid layer when peptide is complexed with a divalent cation.