Constituants amers deBrucea amarissima structures des brucéines A,B et C

Summary Evidence is presented for the structures (II a), (II b) and (II c) for the bruceines A, B and C, the bitter principles isolated from the seeds ofBrucea amarissima.

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18ème Communication sur les constituants amers des Simarubacées; 17ème Communication, voir².     

Isocardenolides

Zusammenfassung Ein einfacher Weg zur Synthese eines von zwei möglichen isomeren Cardenoliden wurde entwickelt und die Reaktionsfolge an Hand der Überführung von Pregnenolon in Isocardenolide V gezeigt.

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Steroids and Related Natural Products XXI. For the previous contribution refer to:G. R. Pettit andP. Hofer, Helv. chim. Acta46, 2142 (1963).

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A preliminary account of this study was presented (December 1963) at the VI. Pan-American Congress of Pharmacy and Biochemistry, Mexico City (Mexico).

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This investigation was supported by PHS Research Grants CY-4074 (C3) to CA-04074-06 from the National Cancer Institute, Public Health Service.     

On the activity of neurosecretory cells in the flesh-flySarcophaga bullata

Résumé L'activité des cellules neurosécretrices dans le cerveau de la femelle deSarcophaga bullata est en corrélation avec le développement des larves dans la femelle et leur position.     

粗粒度并行遗传算法收敛性分析及优化运算

提出了一种新型的粗粒度并行遗传算法(CGGA)，该算法利用多个子种群基于不同的编码方式进行进化计算．首先各子群体独立进行交叉、变异和选择遗传操作，每代进化后迁移算子被引入用来进行种群问的信息交流，迁移算子将各个子种群的最优个体替换相邻种群最差个体后继续进化．基于时齐遍历马尔可夫链理论，给出了CGGA各个子种群的概率转移矩阵与其进化概率转移矩阵，证明了以概率1全局收敛．对典型的测试函数CGGA进行了求解．仿真结果表明，本算法的收敛性能优于经典遗传算法(CGA)，可以有效解决CGA的过早收敛问题．     

多孔介质中的大尺度多相渗流

在许多工业和环境应用中，不同时空尺度上的多孔介质中的多相渗流都是一个非常重要的过程。因此，了解确定微尺度上的多相渗流和其反应传递过程，并描述其宏观条件下的运动现象是很必要的。目前描述宏观下的多相渗流现象都是基于由达西定律经验公式得到的毛管压力一饱和度一相对渗透率关系式。然而，这些经验模型并不能完全反映实际的物理现象，尤其是大尺度和非均质介质中渗流问题。     

Ion-solvent interaction from viscosity,apparent molar volume and conductivity data of bromates,iodates and sulphates of potassium and sodium in dioxane-water mixtures at different temperatures

Summary The viscosity, apparent molar volume and conductivity of KBrO₃, NaBrO₃, KIO₃, NaIO₃, K₂SO₄ and Na₂SO₄ at mass fraction of dioxane (10, 20 and 30%) — water mixtures at 30–45°C±0.01°C have been measured. The ions appear to interact and the ion-solvent interaction is of the order BrO ₃ ^– >IO ₃ ^– >SO ₄ ^2– .     

In vitro modulation of rat adipocyte ghost membrane fluidity by cholesterol oxysterols

The effects of cholesterol and cholesterol-derived oxysterols (cholestanone, cholestenone, coprostanone and epicoprostanol) on adipocyte ghost membrane fluidity were studied using a fluorescence depolarization method. The fluorescence anisotropy of the treated membranes was determined using 1,6-diphenyl-1,3,5-hexatriene (DPH) and 1-(4-trimethylammoniumphenyl)-6-phenyl-1,3,5-hexatriene (TMA-DPH). Cholestanone and cholesterol decreased membranes fluidity at both the concentrations tested (10 & 50 M) while the rest of the sterols did not exert any significant effect on membrane fluidity. In the presence of epinephrine, cholestanone partitioned more towards the lipid core but cholesterol partitioning was not affected. The fusion activation energies (E) obtained for membranes preincubated with cholestanone (8.6 kcal/mol) and cholesterol (8.2 kcal/mol) were not significantly different from that of untreated membranes (8.3 kcal/mol). Membranes preincubated with cholestanone and cholesterol did not exhibit any change in lipid phase throughout the temperature range (10–45°C) tested. The sterols were found to inhibit fisetin-induced phospholipid methylation in isolated rat adipocytes in the rank order of cholesterol > epicoprostanol > cholestanone=cholestenone=coprostanone, while basal methylations was unaffected. When adipocytes were preincubated with the sterols before the addition of fisetin, cholestanone and cholestenone showed 74% and 66% inhibition of maximal methylation respectively. These results indicated that cholesterol oxysterols interact differently with rat adipocyte membranes, with cholestanone interacting more with phospholipids located at the inner lipid bilayer (e.g. phosphatidylethanolamine) while cholesterol interacts more with phosphatidylcholine located at the outer lipid bilayer. This differential interaction may cause selective changes in membrane fluidity at different depths of the bilayer and thus may modulate the activities of membrane-bound proteins such as enzymes and receptors.