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991.
氨酯键和脲键对嵌段聚氨酯和嵌段聚脲性质影响的研究 总被引:2,自引:0,他引:2
用溶液聚合法合成了四种聚氨酯、聚脲模型化合物.并用凝胶渗透色谱,应力—应变,广角X射线衍射等手段检验了在相界面或在硬段微区,不同键对聚合物分子量、力学性质和聚合物形态的影响. 相似文献
992.
本文将文献[3]的引理1推广到s-单式环上,并用迭代技术给出文献[4]的定理2一个简易的证明,将若干有1环的交换性定理推广到s-单式环上。 相似文献
993.
994.
本文得到了拟环满足条件xy=xy ̄(n(x,y)x或xy=yx ̄(n(x,y)y的分解定理。 相似文献
995.
本文阐述了水轮机变结构变参数调速控制的基本问题,提出了相应的控制策略,并论证该控制策略的稳定性、最优性。仿真结果表明本文提出的策略控制效果优良。 相似文献
996.
本文提出了智能化自完善控制策略,通过采用“知识库”存贮最佳的知识与经验,根据受控对象当前运行条件及状态,运用相应的分析逻辑及推理功能,实时地调整控制器结构及参数,以实现逐步改善控制系统性能的目的.文中将所论述的控制策略用于水轮机调速器开发研究. 相似文献
997.
998.
GM-CSF induces human neutrophil IgA-mediated phagocytosis by an IgA Fc receptor activation mechanism 总被引:11,自引:0,他引:11
Immunoglobulin A is the primary immunoglobulin isotype in tears, saliva, breast milk and other mucosal secretions, constituting between 6% and 15% of the total serum immunoglobulins. Human peripheral blood neutrophils have IgA receptors, but these cells do not normally participate in IgA-mediated phagocytosis. The haematopoietic factors granulocyte-macrophage colony-stimulating factor (GM-CSF) and granulocyte colony-stimulating factor (G-CSF) prime neutrophils to be more responsive to a variety of stimuli. We therefore studied their effect on IgA-mediated phagocytosis. GM-CSF and G-CSF both induce a change from low to high-affinity neutrophil IgA Fc crystallizable fragment receptors within 30 min; a change which is associated with the development of IgA-mediated phagocytosis. Human IL-3, which does not affect neutrophil function, is inactive in this system. These results define a new mechanism for CSF-augmented host defence whereby neutrophil function can be modulated by CSF-mediated IgA Fc receptor activation. 相似文献
999.
A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors 总被引:98,自引:0,他引:98
P Ponte P Gonzalez-DeWhitt J Schilling J Miller D Hsu B Greenberg K Davis W Wallace I Lieberburg F Fuller 《Nature》1988,331(6156):525-527
The amyloid proteins isolated from neuritic plaques and the cerebrovasculature of Alzheimer's disease are self-aggregating moieties termed A4 protein and beta-protein, respectively. A putative A4 amyloid precursor (herein termed A4(695] has been characterized by analysis of a human brain complementary DNA. We report here the sequence of a closely related amyloid cDNA, A4(751), distinguished from A4(695) by the presence of a 168 base-pair (bp) sequence which adds 57 amino acids to, and removes one residue from, the predicted A4(695) protein. The peptide predicted from this insert is very similar to the Kunitz family of serine proteinase inhibitors. The two A4-specific messenger RNAs are differentially expressed: in a limited survey, A4(751) mRNA appears to be ubiquitous, whereas A4(695) mRNA has a restricted pattern of expression which includes cells from neuronal tissue. These data may have significant implications for understanding amyloid deposition in Alzheimer's disease. 相似文献
1000.
Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease 总被引:104,自引:0,他引:104
R E Tanzi A I McClatchey E D Lamperti L Villa-Komaroff J F Gusella R L Neve 《Nature》1988,331(6156):528-530
Amyloid B-protein/amyloid A4 is a peptide present in the neuritic plaques, neurofibrillary tangles and cerebrovascular deposits in patients with Alzheimer's disease and Down's syndrome (trisomy 21) and may be involved in the pathogenesis of Alzheimer's disease. Recent molecular genetic studies have indicated that amyloid protein is encoded as part of a larger protein by a gene on human chromosome 21 (refs 6-9). The amyloid protein precursor (APP) gene is expressed in brain and in several peripheral tissues, but the specific biochemical events leading to deposition of amyloid are not known. We have now screened complementary DNA libraries constructed from peripheral tissues to determine whether the messenger RNA encoding APP in these tissues is identical to that expressed in brain, and we identify a second APP mRNA that encodes an additional internal domain with a sequence characteristic of a Kunitz-type serine protease inhibitor. The alternative APP mRNA is present in both brain and peripheral tissues of normal individuals and those with Alzheimer's disease, but its pattern of expression differs from that of the previously reported APP mRNA. 相似文献