Journal of capillary electrophoresis最新文献_第10页

Approaches to detect the drug resistance in acute leukemia 急性白血病耐药检测方法探讨

Journal of capillary electrophoresis Pub Date : 2005-12-01 DOI: 10.2198/JELECTROPH.49.85

T. Funato, Mayu Takeda

引用次数: 2

Assessment of filter plates for multi-well in-gel digestion of proteins separated by polyacrylamide gel electrophoresis to identify them with LC-ESI / MSMS 评价聚丙烯酰胺凝胶电泳分离蛋白的多孔凝胶内酶切滤板的LC-ESI / MSMS鉴定

Journal of capillary electrophoresis Pub Date : 2005-09-01 DOI: 10.2198/JELECTROPH.49.71

K. Kameyama, Tomohiro Nanri, Y. Yamanaka, M. Arima, H. Kawasaki

引用次数: 0

Protein profile of silkworm midgut of fifth-instar day-3 larvae 家蚕5龄第3天幼虫中肠蛋白谱

Journal of capillary electrophoresis Pub Date : 2005-06-01 DOI: 10.2198/JELECTROPH.49.61

H. Kajiwara, Yoko Ito, A. Imamaki, Masatoshi Nakamura, K. Mita, M. Ishizaka

引用次数: 21

Concordance between results of serum protein electrophoresis of pathological serum by cellulose acetate and capillary zone electrophoresis 病理血清醋酸纤维素蛋白电泳结果与毛细管区带电泳结果的一致性

Journal of capillary electrophoresis Pub Date : 2005-06-01 DOI: 10.2198/JELECTROPH.49.45

H. Ihara, Takayuki Matsumoto, Takashi Kakinoki, Y. Aoki, N. Hashizume, Yoshinobu Inada, S. Nanba, G. Yoshino, Mitsutaka Yoshida

{"title":"Concordance between results of serum protein electrophoresis of pathological serum by cellulose acetate and capillary zone electrophoresis","authors":"H. Ihara, Takayuki Matsumoto, Takashi Kakinoki, Y. Aoki, N. Hashizume, Yoshinobu Inada, S. Nanba, G. Yoshino, Mitsutaka Yoshida","doi":"10.2198/JELECTROPH.49.45","DOIUrl":"https://doi.org/10.2198/JELECTROPH.49.45","url":null,"abstract":"We investigated whether the electrophoretic patterns and clinical information derived from the five principal fractions of the Beckman Paragon capillary zone electrophoresis (CZE) 2000 system are comparable to the results obtained by the cellulose acetate electrophoresis (CAE: Olympus AES 320) system. Concordance studies between the results obtained by CAE and CZE were performed on sera from pregnant women and from patients with nephrotic syndrome, acute and chronic inflammatory diseases, cirrhosis, monoclonal and polyclonal gammopathy, and bisalbuminemia. In all subjects except for the pregnant women, the results of CAE and CZE agreed 100% in terms of percent composition for albumin, and α1- and α2-globulins. Concordance for γ-globulin was 92-100% in terms of both percent composition and absolute concentration. Three discordant cases according to the results for β-globulin by CAE and CZE were found in patients with monoclonal gammopathy, who also showed discordant results for γ-globulin. An M-protein spike observed in either the β-globulin or γ-globulin fraction was 100% detected by both CAE and CZE analyses. In another six discordant cases for the β-globulin fraction observed in patients with cirrhosis and polyclonal gammopathy, part of the tail of the β-globulin fraction tended to be measured as γ-globulin by CAE. In three of the four bisalbuminemia cases, the double band of albumin observed by CZE was not detected by CAE. The results show that the electrophoretic patterns and clinical information derived from the five principal fractions of the Beckman Paragon CZE 2000 system are comparable to the results obtained by classical CAE.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"29 1","pages":"45-51"},"PeriodicalIF":0.0,"publicationDate":"2005-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81311770","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 1

Differential expression of aldose reductase in TNF-α responsive rat hepatoma cell lines 醛糖还原酶在TNF-α应答大鼠肝癌细胞系中的差异表达

Journal of capillary electrophoresis Pub Date : 2005-06-01 DOI: 10.2198/JELECTROPH.49.39

Yumiko Hashimoto

引用次数: 0

Mobility-moment analysis of protein-ligand interactions using a multi-capillary electrophoresis instrument : Competitive affinophoresis of concanavalin A and trypsin 利用多毛细管电泳仪分析蛋白质-配体相互作用的流动力矩:豆豆蛋白a和胰蛋白酶的竞争性亲和电泳

Journal of capillary electrophoresis Pub Date : 2005-06-01 DOI: 10.2198/JELECTROPH.49.53

K. Shimura, Takuma Waki, Masaki Okada, T. Toda, Izumi Kimoto, K. Kasai

{"title":"Mobility-moment analysis of protein-ligand interactions using a multi-capillary electrophoresis instrument : Competitive affinophoresis of concanavalin A and trypsin","authors":"K. Shimura, Takuma Waki, Masaki Okada, T. Toda, Izumi Kimoto, K. Kasai","doi":"10.2198/JELECTROPH.49.53","DOIUrl":"https://doi.org/10.2198/JELECTROPH.49.53","url":null,"abstract":"The utility of an automated 96-capillary electrophoresis instrument equipped with a laser-induced fluorescence detector was evaluated in the analysis of affinophoresis using concanavalin A and trypsin as models. Affinophores for concanavalin A and trypsin were prepared by coupling the affinity ligands, p-aminophenylmannoside and p-aminobenzamidine to soluble succinylpolylysine, respectively at a density of about 1/5 of the carboxyl groups. A dual buffer system, 60 mM borate-Na (pH 9.35) as an electrophoresis buffer and 60 mM 3-morpholinopropanesulfonic acid-Na (pH 7.35) containing 0.1% Tween 20 as a sample buffer, was employed to allow the interactions to occur at a physiological pH and also to maintain a high level of electroosmosis and reproducibility in the bare silica capillaries. The electrophoresis of the fluorophore-labeled proteins was carried out in the presence of affinophores, and changes in the mobility of the labeled proteins were analyzed in terms of the mobility moment, which represents the average mobility of the proteins, thus permitting the dissociation constants for the protein-affinophore interactions to be determined. The affinophoresis system was then used to evaluate the extent of binding of low molecular mass compounds based on the inhibition of the affinophoresis. In combination with the mobility moment analysis and the dual buffer system, the multi-capillary electrophoresis instruments proved to be useful for the analysis of biomolecular interactions by electrophoresis.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"13 1","pages":"53-60"},"PeriodicalIF":0.0,"publicationDate":"2005-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88176914","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

2-D LC-MS/MS Analysis of secreted proteins from HepG2 cells: Combination with various sample preparation methods before in-solution trypsin digestion HepG2细胞分泌蛋白的二维LC-MS/MS分析:溶液胰酶消化前不同样品制备方法的结合

Journal of capillary electrophoresis Pub Date : 2005-03-01 DOI: 10.2198/JELECTROPH.49.1

Ryo Yamashita, Y. Fujiwara, Xunmei Yuan, K. Yasuda, Y. Kaburagi

{"title":"2-D LC-MS/MS Analysis of secreted proteins from HepG2 cells: Combination with various sample preparation methods before in-solution trypsin digestion","authors":"Ryo Yamashita, Y. Fujiwara, Xunmei Yuan, K. Yasuda, Y. Kaburagi","doi":"10.2198/JELECTROPH.49.1","DOIUrl":"https://doi.org/10.2198/JELECTROPH.49.1","url":null,"abstract":"Two-dimensional liquid chromatography coupled with tandem mass spectrometry (2-D LC-MS/MS) technique has high capability of resolving peptides, and is used for analysis of tryptic peptides derived from highly complex protein mixtures such as plasma. However, the detection of low-abundant proteins and low-molecular-weight proteins is often very difficult in this system, because major peptides from high-abundant proteins such as albumin mostly disturb the separation of minor peptides from low-abundant proteins. To resolve these problems, different methods of sample preparation for in-solution trypsin digestion were tested, and the optimized method was applied to the 2-D LC-MS/MS analysis of proteins secreted from human hepatoma cell line, HepG2. We could identify 247 and 142 proteins from the chemically and thermally denatured samples, respectively. Among them, 71 proteins were identified in common to both methods, while most of the proteins were identified using either of the two procedures. In addition to these denaturation methods, the molecular-mass cutoff via ultrafiltration improved the efficiency in identifying low-molecular-weight proteins. Finally, we could identify 478 secreted proteins in total using the combination of these processes. These data indicate that in sample preparation the combination of various denaturation methods, as well as molecular-mass cutoff, are very critical for the identification of a wider range of low-abundant proteins via 2-D LC-MS/MS analysis.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"8 1","pages":"1-4"},"PeriodicalIF":0.0,"publicationDate":"2005-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90112631","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Two-dimensional electrophoretic analysis of disease-associated proteins in human cerebrospinal fluid from patients with rheumatoid arthritis 类风湿性关节炎患者脑脊液中疾病相关蛋白的二维电泳分析

Journal of capillary electrophoresis Pub Date : 2005-03-01 DOI: 10.2198/JELECTROPH.49.23

Yukio Yamamoto, Y. Akita, Shigeyuki Tai, S. Fukasaku, Teruhide Yamaguchi, T. Oshizawa, K. Yamaoka, M. Shimamura, T. Hazato

{"title":"Two-dimensional electrophoretic analysis of disease-associated proteins in human cerebrospinal fluid from patients with rheumatoid arthritis","authors":"Yukio Yamamoto, Y. Akita, Shigeyuki Tai, S. Fukasaku, Teruhide Yamaguchi, T. Oshizawa, K. Yamaoka, M. Shimamura, T. Hazato","doi":"10.2198/JELECTROPH.49.23","DOIUrl":"https://doi.org/10.2198/JELECTROPH.49.23","url":null,"abstract":"Comparing protein expression in the cerebrospinal fluid (CSF) of rheumatoid arthritis (RA) patients with that of controls, makes possible the uncovering of proteins that affect disease progression and regulate responsiveness to drugs. Two-dimensional gel electrophoresis (2-DE) and silver staining were used for identifying disease-associated CSF proteins in RA patients. First, to enhance the detection of CSF proteins and to improve the separation of their isoforms by 2-DE, CSF samples were pre-treated with an albumin and IgG removal kit, then by acetone precipitation. The 2-DE analysis revealed more than 1600 spots by the removal of albumin and immunoglobulin from CSF. The expression of the protein spots was not greatly changed in either group, but some notable changes in protein spots were observed in two RA samples. In particular, the expression of an approximately 50 kD protein increased markedly, whereas that of two sequential protein spots of 10-15 kD and with neutral pI decreased in the RA samples. These preliminary results suggest that the proteomic method is conducive to clarifying the mechanism of RA crises, and that some of the expression-changed proteins may be new candidates for disease-associated proteins of RA.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"1 1","pages":"23-27"},"PeriodicalIF":0.0,"publicationDate":"2005-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83028335","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Collaborative proteomics framework with XML databases and an integrated XML viewer for 2DPAGE 协同蛋白质组学框架与XML数据库和集成的XML查看器为2DPAGE

Journal of capillary electrophoresis Pub Date : 2005-03-01 DOI: 10.2198/JELECTROPH.49.35

H. Morisawa, H. Hisatomi, M. Hirota, T. Toda

引用次数: 2

Application of peptides as reaction specific probes for the automated mass spectrometry-assisted enzyme screening (MES) 多肽作为反应特异性探针在自动质谱辅助酶筛选中的应用

Journal of capillary electrophoresis Pub Date : 2005-03-01 DOI: 10.2198/JELECTROPH.49.29

Shenge Ahmed, J. Thiemann, Sandra Kurzawski, Jana Rykl, J. Jankowski, B. Wittmann-Liebold, T. Pohl, H. Schlüter

{"title":"Application of peptides as reaction specific probes for the automated mass spectrometry-assisted enzyme screening (MES)","authors":"Shenge Ahmed, J. Thiemann, Sandra Kurzawski, Jana Rykl, J. Jankowski, B. Wittmann-Liebold, T. Pohl, H. Schlüter","doi":"10.2198/JELECTROPH.49.29","DOIUrl":"https://doi.org/10.2198/JELECTROPH.49.29","url":null,"abstract":"Peptides play a central role as reaction specific probes for screening protein libraries for target enzymes with protein-modifying activities with the automated platform technology named mass spectrometry assisted enzyme screening (MES). The protein libraries are generated by fractionating protein extracts and by immobilizing the proteins covalently to activated affinity beads. The innovative idea of the MES-system is to incubate the fractions of the protein library with special designed peptides that serve as substrates for protein modifying enzymes and to detect the resulting reaction products by mass spectrometry, if the target enzyme is present in a fraction of the protein library. The peptide sequences, selected for the reaction specific probes, are usually parts of the endogenous protein substrates. The main advantage of the MES approach is that even complex protein mixtures can be screened for enzymatic activities. The MES technique is suited for the search for unknown target enzymes with defined catalytic reaction profiles, for investigating the metabolism of defined substrates in cells or tissues and for comparing defined enzyme activities in organisms in different states. Therefore the application of the MES system includes a wide area, from the identification of new drug targets to the identification of enzymes relevant for biotechnological processes. Here the MES system is demonstrated for the screening for urotensin-II (U-II) metabolising enzymes in renal tissue. With MES des-Val-U-II was determined as major metabolite of U-II of renal tissue proteins.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"85 1","pages":"29-34"},"PeriodicalIF":0.0,"publicationDate":"2005-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74035401","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0