抗菌素所致的药物热20例临床分析

近年来抗菌素引起的药物热并不少见，其诊断不易，常误诊为原感染未被控制，致患者发热更高或发生其它过敏症状，如不能及时诊断和停用致热药物，则可能引起严重后果，甚至危及患者生命，故临床医师对抗菌素药热应该熟悉，并应予足够重视。     

SMZ—TMP对大豆幼苗生长的影响

ＳＭＺ－ＴＭＰ溶液浸种，明显促进大豆幼苗生长，增强根系活力，适宜浓度为０．５－１．０ｍｇ／Ｌ。     

替考拉宁工业分离色谱条件选择

讨论了糖肽类抗菌素(替考拉宁)工业分离色谱条件,对参数进行了系统的测试与优化,柱的尺寸为5cm×10cm,流动相为甲醇和水(体积比60∶40,pH值6-7),固定相为C18,6nm;进样体积15mL及进样流速20mL/min等.结论为采用模拟移动床分离提供了基础.     

农用抗生素研究进展

全国农用抗生素学术会议1991年11月4日至7日在浙江桐庐召开,会上交流的74篇学术论文和12篇综述,全面反应了近年来农用抗生素领域国内外研究进展,现本文分三方面加以报道。     

Affinity ultrafiltration of DNA topoisomerases-targeted compounds determined with HPLC／ESI-MS for drug candidate screening

A method of screening assay is demonstrated. The approach is based on the affinity of antitumor candidates for topoisomerases. In this method, antitumor candidates are fished out using topoisomerases as targets. Traditional analysis of complex compounds typically encounters signal suppression due to the relatively low concentrations, but enzyme-affinity screening for the active compounds can effectively concentrate the desired analysts into a small volume of high concen-tration. Active compounds are separated from non-affinity compounds by ultrafiltration. The molecules-enzymes complexes that are retained on the filter are subsequently separated by acidification to obtain the topoisomerases-affinity compounds for analysis on High Performance Liquid Chromatography coupled with electrospray ionization mass spectrometric detec-tion (ESI-MS). This enzyme-affinity based screening assay provides a highly specific and efficient method that can directly screen, identify, and acquire drug candidates thus improving the accuracy and speed of high-throughput screening activities.     

Analysis of proteins that interact with nucleocapsid protein of SARS-CoV using 1 5-mer phage-displayed library

Analysis of proteins that interact with N protein of SARS-CoV using 15-mer phage-displayed library will help to explore the virus pathogenesis and to develop new drugs and vaccines against SARS. In this study, we cloned, expressed and purified N protein of SARS-CoV. This 46-kD N protein was verified by SDS-PAGE and Western-blot. Then, the peptides binding-specific to N protein were identified using 15-mer phage-displayed library. Surprisingly, all of the 89 clones from monoclonal ELISA were positive （S/N〉2.1） and the result was further confirmed experimentally once again. Six N protein-binding peptides, designated separately as SNA1, SNA2, SNA4, SNA5, SNA9 and SNG11, were selected for sequencing. Sequence analysis suggested that SNA5 shared approximatively 100% sequence identity to SNA4, SNA2, SNA9 and SNA1. In addition, the binding specificity of the 15-mer peptides with the SARS-CoV N protein was further demonstrated by blocking ELISA using the synthetical 15-mer peptide according to the deduced amino acid sequence of SNA5. Also, the deduced amino sequence of SNA5 was compared with proteins in translated database using the tblastx program, and the results showed that the proteins with the highest homology were Ubiquinol-cytochrome c reductase iron-sulfur subunits （UCRI or UQCR）, otherwise known as the Rieske iron-sulfur proteins （RISP）. Notablely, in the [2Fe-2S] redox centre of UCRI, there were 6 residues [GGW（Y）F（Y）CP] compatible to the residues （position 2→7, GGWFCP7） of the NH2-terminal of the 15-mer peptide, which indicated higher binding specificity between the N protein of SARS-CoV and the redox centre of UCRI to some extent. Here, the possible molecular mechanisms of SARS-CoV N protein in the pathogenesis of SARS are discussed.