在水生与气生状态下石莼光合作用对光照和温度的响应

如何对付由于高潮时的水生状态与低潮时的气生状态高频率循环所导致的不同环境条件,是潮间带海藻的光合作用所面临的独特问题。对采自汕头沿岸的石莼(Ulva lactuca)在水生和气生不同状态下光合作用对光照和温度的响应特性进行了测定,以探讨这种常见的潮间带绿藻在潮汐循环背景下的光合特性。在气生状态下,光饱和净光合速率(Pmax)随气生暴露时间的变化模式可以很好地用三次方程进行描述,而温度影响方程的系数;当水分损失为15％时,石莼的Pmax增加至最大值,然后Pmax随进一步脱水而下降,在水分损失为80％时下降至0。温度对Pmax的影响在水生状态下比在气生状态下更大。气生状态下（充分水化）Pmax在10℃时显著小于水生状态下的值,而在30℃时则相反。在10℃时,气生干出时间在6 h 以内,或在20℃时,气生干出时间在2.2 h 以内,石莼的净碳固定量在气生状态下比在水生状态下要大;而在30℃时,在气生状态下的净碳固定量比总是小于在水生状态下的净碳固定量。认为石莼在低潮气生状态下与在高潮水生状态下光合特性及净碳固定存在差异,但这种差异与环境温度及叶状体的水分状态有关。     

动物“恋”歌

在蔚蓝的天空下,在葱绿的原野上,在荡漾的湖泊中,鸟儿在比翼双飞中享受快乐的时光,痴情的狼成对奔跑在无尽的旷野,被人唾弃的狐狸其实是典型的情种,鸳鸯的不离不弃成为古今中外歌颂的主题,这些自然界最美丽动人的画卷     

北柴胡营养器官中主要化学成分的组织化学定位及其含量比较

应用植物解剖学、组织化学定位和植物化学方法,研究了北柴胡各营养器官中柴胡皂苷和黄酮类化合物的积累分布状态及其含量变化。结果表明,柴胡皂苷在根中分布在中柱鞘和次生韧皮部中;在茎中主要分布在表皮、棱角处的厚角组织以及位于皮层和髓中的分泌道的上皮细胞中;在叶中,则分布在表皮细胞和整个叶肉组织中。而黄酮类化合物在茎中分布在表皮、棱角处的厚角组织、皮层、髓射线和髓鞘细胞中;在叶中,则主要分布在表皮和位于上下表皮内的厚角组织中。同时,北柴胡中柴胡总皂苷在根、茎、叶中的含量的变化规律为根>叶>茎;而总黄酮在根、茎、叶中的含量的变化规律为叶>茎>根;且在叶中含量相当高,从而为北柴胡的综合利用提供依据,对合理利用药材和保护北柴胡资源也有一定意义。     

春天的脚步

三月是大地回暖、鸟语花香、春光明媚的季节,历经严冬的考验,春日的阳光照在身上倍觉温暖。在这里,我们满怀喜悦地告诉大家,在众多编委的大力支持下,截至二月底的统计显示,《学报》在2011年最初两个月中被引用的情况已经创造了历史最好记录。在过去十年中,《学报》     

国外动态

美国发现可在有氧条件下生产H2的细菌美国华盛顿大学等机构研究人员在英国《自然:通讯》杂志上发表报告说,他们发现1种细菌可以在有O2存在的自然条件下生产H2,有望成为较廉价的H2来源。这种名为"蓝藻菌51142"的细菌在白天和夜晚的生理活动不同。在白天有光线的时候,它可以进行光合作用,生成O2和糖分;而在夜晚,它会燃烧白天生     

恐龙蛋壳的生物力学性质(Ⅵ)──在外力作用下恐龙蛋壳结构的稳定性

应用薄壳理论分析五种类型恐龙蛋壳的受力特性,求出它们在不同状态下埋在沙土中的失稳临界载荷。结果表明,不同类型恐龙蛋在蛋窝中的不同排列方式是与其蛋壳的抗失稳能力的大小密切相关,是某些类群的恐龙在产卵时为解决其低强度蛋壳在保护卵不受外力损伤和在卵的孵化后期幼雏能够破壳而出这两方面的矛盾而采取的一种保护性措施。     

保护地球上最后的大象

大象——世界上最大的陆地哺乳动物。它们的祖先在几千万年前就生存在这个不断演变的星球上。这些庞然大物的家族曾经兴旺发达：地球上一度同时有11种不同的大象在四处漫游,而今天,只有非洲象和亚洲象仍在生存。     

美国研究人员利用老鼠细胞制成“人造水母”

美国哈佛大学和加州理工学院的研究人员在《自然·生物技术》杂志刊登报告说利用硅树脂和老鼠心肌细胞制造出了“人造水母”,它在电流的刺激下能够在水中像水母那样游动,这个“人造水母”的外形像一朵八瓣花,8个“花瓣”都是由硅树脂制成,在它的中心是附着在薄膜上的老鼠心肌细胞。     

中国新记录──小金色藻在武汉东湖的季节消长

一种未曾在中国报道过的小金色藻(Chrysochromulina parva Lackey)在武汉东湖发现,此种在冬季出现,春末消失,高的种群密度(8357.6cells/ml及8737.0cells/ml)分别在1991年2月及1992年1月在水温为6─8℃时形成,持续时间近1个月,小金色藻的生物量在东湖营养状况不同的三个采集站是不同的,但季节消长的趋势基本上一致。此种喜生长在富营养的水体中。       

细菌转座子及其在基因工程中的应用

一、什么叫转座子 转座子是一种能在细胞内不同DNA间转移的DNA序列。在本世纪40年代,美国遗传学家B.McClintok就在玉米中发现了这种遗传因子,她发现玉米的有些基因活性是受一些能在不同染色体间运动的遗传因子所控制的。     

Leucine and tryptophan metabolism in rats.

The rate of tryptophan metabolism in isolated liver cells from animals fed on a high-leucine diet was greater than for cells from control animals. Leucine inhibited tryptophan metabolism and tryptophan uptake in isolated liver cells, probably by competing for membrane transport. Leucine had no effect on tryptophan 2,3-dioxygenase in vitro. 4-Methyl-2-oxovalerate increased tryptophan oxidation in incubations containing albumin, by displacing bound tryptophan and increasing the availability of the amino acid to the cell. The results suggest that, under extreme conditions, when the availability of tryptophan is low, leucine may be pellagragenic.     

Effect of zinc,phosphorus and nitrogen on tryptophan concentration in rice grains grown on limed and unlimed soils

Summary The effects of Zn, P, N and CaCO₃ on tryptophan concentration in rice grain were studied in greenhouse at Haryana Agricultural University. Zinc application upto 20 ppm increased tryptophan concentration in rice grain. Zn-EDTA gave highest increase followed by ZnSO₄ and then ZnO. Liming at the rate of 4 and 8 per cent decreased tryptophan concentration significantly. Phosphorus application upto 100 ppm also decreased tryptophan significantly but Zn in combination with P increased tryptophan and overcame negative effect of P. Nitrogen application upto 120 ppm increased tryptophan concentration. There was positive interaction between Zn and N. Ammonium sulphate gave highest tryptophan followed by ammonium nitrate and then urea. The tryptophan concentration ranged between 766 ppm and 2011 ppm in paddy grain. The lowest tryptophan concentration was in the plants treated with 8 per cent lime in absence of added Zn and highest with 10 ppm Zn through Zn-EDTA. Department of Soils.     

Tryptophan catabolism by tryptophan pyrrolase in rat liver. The effect of tryptophan loads and changes in tryptophan pyrrolase activity.

We investigated how changes in tryptophan pyrrolase activity and tryptophan loads affect the breakdown of tryptophan was estimated by injecting rats with [ring-2-14-C]tryptophan and measuring respiratory 14-CO2. We concluded, contrary to previous reports, that induction of tryptophan pyrrolase definitely will increase the rate of tryptophan breakdown. Tryptophan loads also increase tryptophan breakdown even in circumstances where there is no increase in tryptophan pyrrolase activity, presumably by increasing the saturation of the enzyme. After a tryptophan load (50 mg per kg) the increase in liver tryptophan concentration lasts only 30 min. The rapid return of liver tryptophan to normal may be due partly to the high turnover rate of liver tryptophan. We estimate that tryptophan pyrrolase degrades tryptophan in vivo at a rate that is equivalent to the whole liver tryptophan concentration in 7.5 min or less.     

Tryptophan and serotonin metabolism after sustained tryptophan infusion

In an attempt to elucidate the effects of sustained administration of tryptophan on serotonin synthesis and turnover in mammalian brain, mini-osmotic pumps containing tryptophan or vehicle were implanted in albino mice for 24 and 96 h. Despite the extremely low dose of tryptophan administered by these pumps (8–12 mg/kg-day) statistically significant treatment effects were apparent with both treatment durations. Plasma and brain tryptophan concentrations varied in unison, and were inversely related to the tryptophan degradative capabilities of the liver as reflected in tryptophan pyrrolase activity. After 24 h of tryptophan infusion the hepatic enzyme activity was elevated and tryptophan values were no different from controls, and after 96 h the hepatic enzyme activity was reduced and tryptophan values in treated animals were greater than controls. Serotonin was elevated in treated animals after 24 h, but not after 96 h despite the elevated tryptophan concentration at this time. The turnover of serotonin, as evidenced by 5-hydroxyindoleacetic acid concentrations, was not significantly affected by either treatment.Hepatic degradation of tryptophan thus seemed to be an important determinant of total plasma tryptophan, and brain tryptophan values paralleled plasma tryptophan. It appears that serotonin biosynthesis is regulated by factors other than tryptophan availability when the latter is chronically elevated.     

Tryptophan properties in fluorescence and functional stability of plasminogen activator inhibitor 1

Plasminogen activator inhibitor 1 harbors four tryptophan residues at positions 86, 139, 175, and 262. To investigate the contribution of each tryptophan residue to the total fluorescence and to reveal the mutual interactions of the tryptophan residues and interactions with the other amino acids, 15 mutants in which tryptophan residues have been replaced by phenylalanines were constructed, purified, and characterized. Conformational distribution analysis revealed that the tryptophan mutants have a similar conformational distribution pattern as wild-type plasminogen activator inhibitor 1. Mutants in which tryptophan residue 175 was replaced by a phenylalanine displayed an increased functional half-life of the active conformation, whereas the functional half-life of mutants in which tryptophan residue 262 was replaced by a phenylalanine was substantially decreased. Comparative analysis of the fluorescence lifetimes, the extinction coefficients, and the quantum yields of the individual tryptophan residues demonstrates that tryptophan residue 262 gives the highest contribution to the total fluorescence. The other tryptophan residues have a very low quantum yield. In the wild-type protein, the fluorescence of all tryptophan residues is partially quenched as compared to the mutants that contain single tryptophan residues, due to conformational effects. The fluorescence of tryptophan residue 262 is very likely also partially quenched by energy transfer to tryptophan residue 175.     

Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies.

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.     

Intralipid and free plasmatic tryptophan in vitro

In an attempt to investigate the role of the lipidic emulsion Intralipid in the development of metabolic encephalopathy in a patient showing high free tryptophan levels, the relationship between lipidic emulsion and free tryptophan was examined in in vitro experiments. The addition of intralipid to normal serum produces an immediate increase in non-esterified fatty acids and a parallel rise in free tryptophan. Moreover, when serum with intralipid is incubated at 37 degrees C, the lipases release new non-esterified fatty acids and the free tryptophan increases proportionally. The non-esterified fatty acid content of intralipid was found to be 12 +/- 2 mEq X 1(-1). An inverse correlation was seen between free tryptophan and different serum albumin concentrations. It is concluded that intralipid causes an increase in free tryptophan levels. It is known that in vivo free tryptophan modulates 5-hydroxytryptamine synthesis and thus may be considered a possible causal agent for encephalopathy.     

IDO induces expression of a novel tryptophan transporter in mouse and human tumor cells

IDO is the rate-limiting enzyme in the kynurenine pathway, catabolizing tryptophan to kynurenine. Tryptophan depletion by IDO-expressing tumors is a common mechanism of immune evasion inducing regulatory T cells and inhibiting effector T cells. Because mammalian cells cannot synthesize tryptophan, it remains unclear how IDO(+) tumor cells overcome the detrimental effects of local tryptophan depletion. We demonstrate that IDO(+) tumor cells express a novel amino acid transporter, which accounts for ～50% of the tryptophan uptake. The induced transporter is biochemically distinguished from the constitutively expressed tryptophan transporter System L by increased resistance to inhibitors of System L, resistance to inhibition by high concentrations of most amino acids tested, and high substrate specificity for tryptophan. Under conditions of low extracellular tryptophan, expression of this novel transporter significantly increases tryptophan entry into IDO(+) tumors relative to tryptophan uptake through the low-affinity System L alone, and further decreases tryptophan levels in the microenvironment. Targeting this additional tryptophan transporter could be a way of pharmacological inhibition of IDO-mediated tumor escape. These findings highlight the ability of IDO-expressing tumor cells to thrive in a tryptophan-depleted microenvironment by expressing a novel, highly tryptophan-specific transporter, which is resistant to inhibition by most other amino acids. The additional transporter allows tumor cells to strike the ideal balance between supply of tryptophan essential for their own proliferation and survival, and depleting the extracellular milieu of tryptophan to inhibit T cell proliferation.     

Indolic Substances in Plasma, Cerebrospinal Fluid, and Frontal Cortex of Human Subjects Infused with Saline or Tryptophan

Psychiatric patients undergoing the psychosurgical operation of stereotactic subcaudate tractotomy were infused intravenously with either saline or L-tryptophan (15 mg/kg/h). Plasma, lumbar cerebrospinal fluid (CSF), ventricular CSF and a specimen of frontal cortex were collected. The relationships of plasma concentrations of substances claimed to influence brain tryptophan concentration (total tryptophan, free tryptophan, large neutral amino acids) with the concentration of tryptophan in the cortex and CSF were investigated. Tryptophan infusion resulted in plasma tryptophan values comparable to those found after oral doses used in treating depression or insomnia, and about sixfold increases of tryptophan in the cerebral cortex. Increased brain 5-hydroxytryptamine synthesis was indicated by significant rises of CSF 5-hydroxyindoleacetic acid. The concentration of plasma free tryptophan was a better predictor than plasma total tryptophan of cortex tryptophan concentration. As all correlation coefficients of plasma versus brain or plasma versus ventricular CSF tryptophan concentrations were decreased when allowance was made for differences of concentration of large neutral amino acids, the results suggest that the role of these substances within their physiological range as inhibitors of tryptophan transport to the brain may previously have been overemphasised.     

Guinea-pig liver tryptophan pyrrolase. Absence of detectable apoenzyme activity and of hormonal induction by cortisol and possible regulation by tryptophan

1. When assayed in fresh homogenates, guinea-pig liver tryptophan pyrrolase exists only as holoenzyme. It does not respond to agents that activate or inhibit the rat liver enzyme in vitro. Only by aging (for 30min at 5 degrees C) does the guinea-pig enzyme develop a requirement for ascorbate. 2. The guinea-pig liver enzyme is activated by the administration of tryptophan but not cortisol, salicylate, ethanol or 5-aminolaevulinate. 3. The tryptophan enhancement of the guinea-pig liver pyrrolase activity is prevented by 0, 34 and 86% by pretreatment with actinomycin D, cycloheximide or allopurinol respectively. 4. The guinea-pig liver tryptophan pyrrolase is more sensitive to tryptophan administration than is the rat enzyme. On the other hand, the concentrations of tryptophan in sera and livers of guinea pigs are 45-52% less than those in rats. 5. It is suggested that tryptophan may regulate the activity of guinea-pig liver tryptophan pyrrolase by mobilizing a latent form of the enzyme whose primary function is the detoxication of its substrate.