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Search Results: 1 - 10 of 77298 matches for " 伴刀豆球蛋白A "
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ATP对巨噬细胞内吞和溶酶体pH的影响
雷国华,朴英杰,鲍永耀,吴建春
生物物理学报 , 1997,
Abstract: FITC-dextran标记培养的小鼠腹腔巨噬细胞溶酶体,ConA-FITC标记细胞内吞。用激光扫描共聚焦显微镜测量伴刀豆球蛋白(ConA)、ATP引起的巨噬细胞溶酶体pH动态变化和ATP对细胞内吞ConA-FITC的影响。结果显示ConA引起巨噬细胞溶酶体pH迅速增加,6min左右达到峰值(pH5.7);ATP刺激30min后再加入ConA,溶酶体pH无明显变化(pH4.0);同时加入ATP和ConA,5min左右溶酶体pH降到最低点(pH4.1);ATP对巨噬细胞内吞ConA-FITC有明显的抑制作用。探讨了受体介导内吞与溶酶体pH的关系。
Research on the Orientedly Immobilized Urease via Concanavalin A
以伴刀豆球蛋白为介质定向固定化脲酶的研究

Jianqin Zhou,Shaohua Chen,Jianwen Wang,
周建芹
,陈韶华,王剑文

微生物学报 , 2008,
Abstract: Concanavalin A (ConA) is immobilized on a pre-activated chitosan microspheres, and then oriented immobilization of urease is carried out based on the strong interaction between ConA and glycoprotein. The optimum immobilization conditions are as follows: glutaraldehyde concentration is 3.5%, ConA concentration 1mg/mL, ConA pH 7.0 and urease concentration 0.4 mg/mL. For orientedly immobilized urease, the highest activity was allowed at pH 5.0~6.0 and temperature 77°C, and the Michaelis constant (Km) was disclosed to be 11.76 mmol/L by Lineweaver-Burk plot. Compared with the free urease and the randomly immobilized urease, the optimum pH of the orientedly immobilized urease becomes smaller and the pH domain wider. Orientedly immobilized urease presents higher temperature resistance, higher affinity to the substrate, and higher stability of operation.
伴刀豆球蛋白A-糖复合物的模拟分析
吴显辉,郭明雄,冯胜彦,陈蔚梅,艾建宇,吴斌,熊晓然
植物科学学报 , 2003,
Abstract: ?主要分析ConA与不同的糖特异性结合时其活性位点构象变化的特征。模拟分析了ConA糖结合活性中心氨基酸残基结构特征,同时对相应残基原子可及性表面进行了计算和分析。结果表明:(1)ConA在和不同的糖结合时,存在不同的结合方式;(2)不管ConA和什么糖结合,主要的作用是由活性中心的Tyr12、Asn14、Asp208和Arg228提供的;(3)无论是结合单糖还是寡糖,活性中心总是与第一个糖环起主要的结合作用。
基于自组装多层膜的葡萄糖表面等离子体共振传感器
羊小海,黎振华,王青,王柯敏
化学学报 , 2007,
Abstract: 利用伴刀豆球蛋白A和糖类的特异性相互作用,研制了葡萄糖表面等离子体共振传感器.传感器的敏感膜是构建于金膜表面的伴刀豆球蛋白A/葡聚糖自组装多层膜.在葡萄糖的存在下,该自组装多层膜被分解,引起表面等离子体共振信号的显著变化,信号变化的大小与葡萄糖的浓度相关.结果表明,利用该传感器可以选择性地检测0.1~50mmol?L-1浓度范围内的葡萄糖,且敏感膜可以多次再生使用.
伴刀豆球蛋白a中铽(ⅲ)和钴(ⅱ)之间的能量转移——一种新的金属离子之间距离的探针
马贵斌?,杨频?
生物化学与生物物理进展 , 1991,
Abstract:
伴刀豆球蛋白a-糖复合物的模拟分析
吴显辉,郭明雄,冯胜彦,陈蔚梅,艾建宇,吴斌,熊晓然
植物学学报 , 2003,
Abstract: ?主要分析cona与不同的糖特异性结合时其活性位点构象变化的特征。模拟分析了cona糖结合活性中心氨基酸残基结构特征,同时对相应残基原子可及性表面进行了计算和分析。结果表明:(1)cona在和不同的糖结合时,存在不同的结合方式;(2)不管cona和什么糖结合,主要的作用是由活性中心的tyr12、asn14、asp208和arg228提供的;(3)无论是结合单糖还是寡糖,活性中心总是与第一个糖环起主要的结合作用。
COMPARISON OF CHANGES IN MEMBRANE MOLECULE MOTION AND MICROFILAMENT ASSEMBLY UNDER THE ACTION OF ConA AND LN
伴刀豆球蛋白A和层粘连蛋白与膜受体结合下膜分子运动及微丝组装变化的比较

魏新华,苏雅娴,何其华,杨正红,卢景芬,王文玉,付世密
生物物理学报 , 1993,
Abstract: In this paper, we have studied the changes of molecule motion in macrophage membrane and microfilament assembly below membrane after Con A or LN binding with membrane receptors on macrophage. Results showed the decrease of the lateral diffusion velocity of proteins on membrane surface. the reduction of the lipid fluidity of membrane and the increment of microfilament assembly under the action of Con A and LN.
ConA激活小鼠胸腺T淋巴细胞增殖过程中c-myc与核骨架蛋白的结合
曾丛梅,蔡树涛,周凤兰,张锦珠,
中国科学 生命科学 , 1996,
Abstract: 采用DNA-蛋白质体外吸附的方法研究伴刀豆球蛋白激活小鼠胸腺T淋巴细胞增殖过程中c-myc与核骨架蛋白的结合.实验结果显示,c-myc与核骨架蛋白的结合具有特异性,在淋巴细胞激活过程中c-myc与P34/P36核骨架蛋白及核纤层蛋白结合,并发生动态变化.
EFFFCT OF CONA-RECEPTIOR INTERACTION ON THE ACTIN FILAMENT ASSEMBLY IN MACROPHAGE
伴刀豆球蛋白A与巨噬细胞膜受体结合对膜下F-actin的影响

胡良高,高宁红,尹忆民,朱树梅,苏雅娴
生物物理学报 , 1996,
Abstract: Signal fornsduction folloWed by aCtiVation of the Cells could be initined by ligandscombmmg with membrane recrptors. In this paper, the changes of actin polymerization,F-actin organzation and distribution, and thermodynach in macrophage induced byConA-receptor inthection were studied by using confocal laser scanning microscope system.flow cytometry and differential scanning calorimetry.The results showed that when ConA combined with sauce recptor of macrophage, the content of F-actin was inmesed actin filamentS were meshed within the cells and the releasingheat of the Cells was also inCreased. These changes suggestal that the course of actin filamentsassembly and meshwork induce by etnA wiht play an boortant role in signal hansductionand cell activation.
葡萄糖氧化酶复合物电极的研制
叶帮策,李友荣
华东理工大学学报 , 1993,
Abstract: 研究了葡萄糖氧化酶(GoD)和伴刀豆球蛋白A(ConA)复合物的热稳定性,计算了其在不同温度下的热失活常数k_d。实验结果表明,GOD-ConA复合物与GOD相比,可显著提高酶的热稳定性。应用该复合物制作的二茂铁媒介生物传感器,在室温22℃条件下,响应电流在10d后基本没有衰减。
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