Y(RA)3·4H2O的合成及其抗白血病HL-60细胞的研究

在避光、无水、无氧条件下合成了维甲酸钇的配合物,通过元素分析、摩尔电导、红外光谱、紫外光谱、差热及热重分析对配合物的结构和性质进行了表征,其分子式为Y(RA)3@4H2O.采用MTT比色法及NBT还原试验分别研究了该配合物及全反式维甲酸(HRA)对HL-60细胞增殖的影响.结果表明,二者均具有抑制HL-60细胞增殖及诱导其分化的作用,尤其配合物对HL-60细胞的作用很明显,优于全反式维甲酸(P＜0.01).     

TRAF4 functions as an intermediate of GITR-induced NF-κB activation

Members of the tumor necrosis factor receptor (TNFR) family regulate the activation, differentiation, and function of many cell types, including cells of the immune system. TNFR-associated factors (TRAFs) function as adapter molecules controlling signaling pathways triggered by TNFR family members, such as activation of nuclear factor B (NF-B). Despite intensive research, the function of TRAF4 in signaling pathways triggered by TNFR-related proteins remains enigmatic. Intriguingly, our functional studies indicated that TRAF4 augments NF-B activation triggered by glucocorticoid-induced TNFR (GITR), a receptor expressed on T cells, B cells, and macrophages. Further analyses revealed that TRAF4-mediated NF-B activation downstream of GITR depends on a previously mapped TRAF-binding site in the cytoplasmic domain of the receptor and is inhibited by the cytoplasmic protein A20. GITR is thought to inhibit the suppressive function of regulatory T cells (T_reg cells) and to promote activation of T cells. Taken together, our studies provide the first indications that TRAF4 elaborates GITR signaling and suggest that TRAF4 can modulate the suppressive functions of T_reg cells.Received 20 September 2004; received after revision 8 October 2004; accepted 18 October 2004     

水下目标特征提取与分类的C30硬件实验研究

本文针对水下目标识别问题，在Ｃ３０信号处理机上实现了目标特征提取、特征压缩和分类三个环节的几个典型方法，并实验研究了这些方法的性能。结果表明，Ｃ３０处理器能有效地实现复杂的目标识别方法，且各方法表现出良好的识别效果和实时性能，为目标识别技术实际应用提供了重要的依据和实验手段。     

N-未取代的C_(60)吡咯烷衍生物的分离纯化和结构表征(英文)

C60与α-氨基酸和醛酮反应生成N-未取代的C60吡咯烷衍生物。本文给出了用柱层析法分离纯化产物的一般原理和过程，总结了用FD－MS，FT－IR，UV－Vis，1H－NMR和13C－NMR表征产物结构时所给出的共同特征。     

Identification of the bioactive peptide PEC-60 in brain

PEC-60 is a 60-residue peptide originally isolated from pig intestine. It inhibits glucose-induced insulin secretion from perfused pancreas in a hormonal manner and also has biological activity in the immune system. PEC-60-like immunoreactive material has been reported in catecholamine neurons of the central and peripheral nervous systems, but the peptide has not been identified from that material. We have now isolated PEC-60 from pig and rat brains with a method that combines column purification procedures with the specificity of a radioimmunoassay and the sensitivity of mass spectrometry to directly identify the peptide. The results show that PEC-60, like many other peptides, is expressed in the gastrointestinal tract and the central nervous system. The specific regional brain distribution and interaction with classical neurotransmitters raise the possibility that PEC-60may play a role in the central nervous system disorders involving dopamine dysregulation. Received 6 December 2002; received after revision 10 December 2002; accepted 11 December 2002 RID="*" ID="*"Corresponding author.     

Investigation of solvatochromism and aggregation behavior of C_(60)(C_4H_(10)N~+)I~- in binary solvent mixtures

Solvatochromism was observed in some solutions of C60 or C70, which was thought to arise from the formation of fullerene clusters[1—6]. This special type of solvato- chromism has aroused much interest because it has some potential applications in material science and sensor tech- nology. On the other hand, C60 or C70 can be made soluble in water by connecting it to various functional groups[7—20]. Those functionalized fullerenes not only have been found a number of important applicati…     

A simple, economical method of converting gene expression products of insulin into recombinant insulin and its application

A method, by which the gene expression product of recombinant single chain insulin can be converted into insulin by directly digesting with trypsin, has been established. This method has been used in process of porcine insulin precursor (PIP), [B16Ala]PIP and [B26Ala]PIP into (desB30)insulin, (desB30)[B16Ala]insulin and (desB30)[B26Ala]insulin, respectively, and all of them retain full biological activity of that of their corresponding parent, recombinant human insulin, [B16Ala]insulin and [B26Ala]insulin. The results further demonstrate that the C-terminal residue of B chain is not necessary for insulin's biological activity. Compared with the method of transpeptidation, this method is simple, with a high yield, and avoids the use of organic reagents, and in comparison with the trypsin/carboxypeptidase method, it omits the use of carboxylpeptidase. Besides, (desB30)[B16Ala]insulin and (desB30)[B26Ala]insulin still remained without self-association property as that of their parents, which demonstrate that they are monomeric insulin. So they can be used for substituting for monomeric insulin, [B16Ala]insulin and [B26Ala]insulin, in clinical applications.