细旦丙纶针织物湿舒适性研究——常规客观试验方法测试研究

针对国内新近研制开发的细旦丙纶纤维,本文依据服装舒适性理论,运用常规客观测试方法,对细旦丙纶针织物的液态水传递能力、液态水保持能力、透气性能,放湿干燥性能进行了探讨,最后用灰色聚类判别分析法进行了综合评价。     

Étude biochimique des poissons: 1. Variations semestrielles de la teneur en eau et en protéines du tissu musculaire de la truite Arc-en-ciel (Salmo gairdnerii Rich)

Summary The authors have noted, during the reproductive cycle of the Rainbow trout (Salmo gairdnerii Rich), important variations concerning water and total proteins content. This study shows a great correlation between the biological process and biochemical variations.     

Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex

Intimin and its translocated intimin receptor (Tir) are bacterial proteins that mediate adhesion between mammalian cells and attaching and effacing (A/E) pathogens. Enteropathogenic Escherichia coli (EPEC) causes significant paediatric morbidity and mortality world-wide. A related A/E pathogen, enterohaemorrhagic E. coli (EHEC; O157:H7) is one of the most important food-borne pathogens in North America, Europe and Japan. A unique and essential feature of A/E bacterial pathogens is the formation of actin-rich pedestals beneath the intimately adherent bacteria and localized destruction of the intestinal brush border. The bacterial outer membrane adhesin, intimin, is necessary for the production of the A/E lesion and diarrhoea. The A/E bacteria translocate their own receptor for intimin, Tir, into the membrane of mammalian cells using the type III secretion system. The translocated Tir triggers additional host signalling events and actin nucleation, which are essential for lesion formation. Here we describe the the crystal structures of an EPEC intimin carboxy-terminal fragment alone and in complex with the EPEC Tir intimin-binding domain, giving insight into the molecular mechanisms of adhesion of A/E pathogens.     

一个捕食模型非常数正解的存在性

讨论一个带有齐次Neumann边界条件的强耦合捕食模型,给出了非常数正解的存在性.     

一类Schr(o)dinger-Virasoro型李代数中间序列模的分类

主要考虑了一类形变Schr(o)dinger-Virasoro型李代数L的中间序列模,给出了此类模的完全分类.     

Die Hämagglutination des Influenzavirus A2-Hongkong

Summary A₂-Hongkong influenza virus does not agglutinate the erythrocytes of the cow, the calf, the horse, the pony and the spiny mouse at room temperature, while the A₂-Asia influenza virus causes agglutination. At a temperature of 4 °C A₂-Hongkong was able to agglutinate the erythrocytes of all species examined except those of the spiny mouse. Whether the A₂-Hongkong virus does or does not agglutinate the erythrocytes of the chicken, the donkey, the goat, the spiny mouse and the horse at room temperature could depend on the speed of elution.