Inhibition of M-MuLV reverse transcriptase activity by fullerene derivatives

The biological properties and biomedical application of fullerene (C60) and its derivatives are currently very active subjects concerning fullerene research. The bio logical effects of fullerene and its derivatives include enzyme inhibition, sites-selective DNA cleavage, antibacterial and antiviral activities, photocytotoxicity and antiapoptosis[1―4]. Especially, enzymes inhibited by fullerene derivatives mainly consist of oxidation-reduc- tion related enzymes such as glutathione transferase…     

Demonstration by NMR of folding domains in lysozyme

Although there has been much speculation on the pathways of protein folding, only recently have experimental data on the topic been available. The study of proteins under conditions where species intermediate between the fully folded and unfolded states are stable has provided important information, for example about the disulphide intermediates in BPTI, cis/trans proline isomers of RNase A3 and the molten globule state of alpha-lactalbumin. An alternative approach to investigating folding pathways has involved detection and characterization of transient conformers in refolding studies using stopped-flow methods coupled with NMR measurements of hydrogen exchange. The formation of intermediate structures has been detected in the early stages of folding of cytochrome c, RNaseA and barnase. For alpha-lactalbumin, hydrogen exchange kinetics monitored by NMR proved to be crucial for identifying native-like structural features in the stable molten globule state. An analogous partially folded protein stable under equilibrium conditions has not been observed for the structurally homologous protein hen egg-white lysozyme, although there is evidence that a similar but transient state is formed during refolding. Here we describe NMR experiments based on competition between hydrogen exchange and the refolding process which not only support the existence of such a transient species for lysozyme, but enable its structural characteristics to be defined. The results indicate that the two structural domains of lysozyme are distinct folding domains, in that they differ significantly in the extent to which compact, probably native-like, structure is present in the early stages of folding.     

超声激活血卟啉对在体艾氏腹水肉瘤的抑制

利用频率为2.0 MHz,强度为5.0 W/cm2的超声激活血卟啉对在体小鼠艾氏腹水瘤细胞 进行了抑癌作用研究.通过对一次和多次处理的肿瘤体积和重量变化趋势的研究,发现声动力疗法 对艾氏腹水瘤细胞增殖有显著抑制作用,且多次处理比一次处理效果更为明显.     

2-巯基苯并噻唑衍生物自组装分子膜对45#钢的缓蚀性能

合成了2-辛巯基苯并噻唑化合物,运用IR、MS和元素分析等方法对其结构进行了表征。通过自组装技术在钢片表面制备有机分子膜;采用静态失重法和电化学测试技术研究了自组装膜在1mol/LHCl中对钢片的缓蚀性能。结果表明,2-巯基苯并噻唑衍生物缓蚀剂自组装膜对钢片有良好的缓蚀能力。     

Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate

Hen egg-white lysozyme (HEWL) was the first enzyme to have its three-dimensional structure determined by X-ray diffraction techniques. A catalytic mechanism, featuring a long-lived oxocarbenium-ion intermediate, was proposed on the basis of model-building studies. The 'Phillips' mechanism is widely held as the paradigm for the catalytic mechanism of beta-glycosidases that cleave glycosidic linkages with net retention of configuration of the anomeric centre. Studies with other retaining beta-glycosidases, however, provide strong evidence pointing to a common mechanism for these enzymes that involves a covalent glycosyl-enzyme intermediate, as previously postulated. Here we show, in three different cases using electrospray ionization mass spectrometry, a catalytically competent covalent glycosyl-enzyme intermediate during the catalytic cycle of HEWL. We also show the three-dimensional structure of this intermediate as determined by X-ray diffraction. We formulate a general catalytic mechanism for all retaining beta-glycosidases that includes substrate distortion, formation of a covalent intermediate, and the electrophilic migration of C1 along the reaction coordinate.     

壳聚糖的溶菌酶降解

用粘度法和还原糖法研究了溶菌酶降解壳聚糖过程中温度、pH值、时间、酶浓度、底物浓度以及金属离子对降解速度的影响.比较合适的降解条件是:温度45℃,pH值5.0,适当增大酶浓度和底物浓度能够加速壳聚糖的降解,在一定的底物浓度下溶菌酶降解壳聚糖的反应不遵循简单的一级反应动力学.一定浓度的Cu2+、Zn2+、Ba2+、Cr3+能够促进壳聚糖在溶菌酶作用下的降解,而K+、Ca2+和高浓度的Zn2+会抑制酶活力的发挥.     

香草醛对酪氨酸酶活性的抑制

在25℃，pH=6．8的Na2HPO4-NaH2PO4缓冲体系中，采用酶动力学方法研究了香草醛对酪氨酸酶单酚酶和二酚酶活性的抑制效应．实验结果表明：香草醛对酪氨酸酶单酚酶和二酚酶活性均有抑制作用，其半数抑制浓度（IC50）约分别为2．7和4．1mmol／L；香草醛能明显延长单酚酶的迟滞时间，4mmol／L香草醛能使迟滞时间由1．1min延长至3min；Lineweaver-Burk图显示香草醛对二酚酶的抑制作用表现为混合性抑制，对游离酶的抑制常数和对酶-底物络合物的抑制常数分别为3．48和15．1mmol／L．