Journal of capillary electrophoresis最新文献_第9页

全自動電気泳動装置（常光CTE8000）による臨床検査タンパク性能評価全自动电泳装置(常光CTE8000)临床检测蛋白质性能评价

Journal of capillary electrophoresis Pub Date : 2007-01-01 DOI: 10.2198/sbk.51.113

京子宮﨑, 正芳米山, 美穂高橋, 照夫江上, 宏明大西, 卓渡邊

{"title":"全自動電気泳動装置（常光CTE8000）による臨床検査タンパク性能評価","authors":"京子宮﨑, 正芳米山, 美穂高橋, 照夫江上, 宏明大西, 卓渡邊","doi":"10.2198/sbk.51.113","DOIUrl":"https://doi.org/10.2198/sbk.51.113","url":null,"abstract":"Recently a new cellulose acetate membrane for electrophoresis to analyze protein fractions, named SELECA-VSP, was developed by Toyo Roshi Kaisha Ltd. In advance of commercial supply, a study group was organized to investigate utility of this new membrane in comparison with SEPARAX-SP, a standard membrane for protein fraction assay widely used in Japan. As a member of this study group, our laboratory mainly investigated the difference between the two membranes when analyzing protein fractions in serum as well as ascites, pleural fluid, cerebrospinal fluid and urine. JOKO-CTE8000 was used as a protein fraction analyzer. When buffer lacking EDTA was used in electrophoresis of serum and ascites, the correlation efficiency between the two membranes in percentage of the β fraction was inferior to that of other fractions. When EDTA-containing buffer was used in analysis of serum and ascites, however, the correlation between the two membranes in β-fraction was improved to a comparable level to other fractions. The correlations between the two membranes were satisfactory in analysis of samples other than serum and ascites, regardless of the presence of EDTA in buffer. We conclude that this newly developed membrane has the similar performance to a standard membrane and could be applied in assay of protein fraction in clinical samples.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"54 1","pages":"113-117"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78647240","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

新規膜「セレカ-VSP」を用いた血清タンパク分画の評価～全自動電気泳動分析装置CTE-1800（常光）による分析～使用新膜“celeka -VSP”的血清蛋白质分划的评价~根据全自动电泳分析装置CTE-1800(常光)的分析~

Journal of capillary electrophoresis Pub Date : 2007-01-01 DOI: 10.2198/sbk.51.119

和代中村, 秋恵須郷, 栄治宮島

引用次数: 0

Efficient electroblotting of gel-resolved proteins onto diamond-like carbon-coated plate for protein-chip 高效电印迹凝胶溶解蛋白质到类金刚石碳涂层板的蛋白质芯片

Journal of capillary electrophoresis Pub Date : 2006-12-01 DOI: 10.2198/JELECTROPH.50.33

Yoko Ino, Akiko Okayama, Y. Iwafune, Noriaki Arakawa, J. Kikuchi, M. Kamita, H. Kawasaki, Takeshi Okada, H. Hirano

{"title":"Efficient electroblotting of gel-resolved proteins onto diamond-like carbon-coated plate for protein-chip","authors":"Yoko Ino, Akiko Okayama, Y. Iwafune, Noriaki Arakawa, J. Kikuchi, M. Kamita, H. Kawasaki, Takeshi Okada, H. Hirano","doi":"10.2198/JELECTROPH.50.33","DOIUrl":"https://doi.org/10.2198/JELECTROPH.50.33","url":null,"abstract":"We have developed a technique, which can produce high-density protein chips. In this technique, proteins are separated by gel electrophoresis, and electroblotted by semidry blotting apparatus onto a diamond-like carbon-coated stainless-steel plate (DLC plate) of which surface is modified chemically with amino groups. Proteins immobilized on this protein chip can interact with other proteins in solution, and proteins interacted with the immobilized proteins can be identified by mass spectrometric analysis. However, the electroblotting efficiency was not stable. We anticipated that the unstable efficiency might be related to the fluctuation of temperature during electroblotting. In the present study, to investigate the optimal temperature for efficient and effective electroblotting, we developed a semidry blotting apparatus, which could regulate blotting temperature from 4 to 45°C (±1°C). The high and reproducible blotting efficiency was obtained at not low temperature but rather high temperature (30°C). The temperature did not impede protein identification or analysis of protein-protein interactions on the DLC plates by mass spectrometry.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"10 1","pages":"33-37"},"PeriodicalIF":0.0,"publicationDate":"2006-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87014386","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

Draft of silkworm proteome database 家蚕蛋白质组数据库草案

Journal of capillary electrophoresis Pub Date : 2006-12-01 DOI: 10.2198/JELECTROPH.50.39

H. Kajiwara, K. Nakane, Jiang Piyang, A. Imamaki, Yoko Ito, Fumio Togasaki, Tsuyoshi Kotake, Hikari Murai, Masatoshi Nakamura, K. Mita, R. Nomura, Yuji Shimizu, Michihiko Shimomura, M. Ishizaka

引用次数: 9

Micro two-dimensional electrophoretic analysis of changes in plasma proteins of next-generation rat of the pregnant rats administered to coplanar PCBs 共面多氯联苯对妊娠大鼠下一代血浆蛋白变化的微二维电泳分析

Journal of capillary electrophoresis Pub Date : 2006-12-01 DOI: 10.2198/JELECTROPH.50.25

K. Sakaguchi, J. Suzuki, Masaki Tanaka, M. Shirai, F. Akahori

{"title":"Micro two-dimensional electrophoretic analysis of changes in plasma proteins of next-generation rat of the pregnant rats administered to coplanar PCBs","authors":"K. Sakaguchi, J. Suzuki, Masaki Tanaka, M. Shirai, F. Akahori","doi":"10.2198/JELECTROPH.50.25","DOIUrl":"https://doi.org/10.2198/JELECTROPH.50.25","url":null,"abstract":"Polychlorinated biphenyl (PCB) 126 or PCB 169 was administered to pregnant rats and kinetic changes in plasma protein spots of their next generation (F2 rats) ages 1, 3, 6, and 15 weeks were observed by micro two-dimensional polyacrylamide gel electrophoresis (M2D-PAGE). In the control group in which age-related changes were observable, changes in the form of the albumin (Alb) spot were recognized at ages 1-3 weeks. Only the Alb spot on the acid side, i.e., non-mercaptoalbumin, was recognized at age 1 week. At age 3 weeks, the Alb spot on the alkaline side, i.e., mercaptoalbumin, also became observable. On the other hand, qualitative changes in the form of Alb, i.e., manifestations of mercaptoalbumin, were recognized at age 1 week by administration of PCB 126. This result suggested that the influence of PCB 126 on the living body is greater than that of PCB 169. In spite of the treatment for toxicity by equivalence of dose control on the basis of toxicity equivalency factor (TEF) 0.1 for PCB 126 (PeCB) and 0.01 for PCB 169 (HxCB), the influence of PCB 126 on the living body was greater than that of PCB 169. The C3 spot was increased at age 3 weeks in the PCB 126 and the PCB 169. The spot showed a tendency toward increase at age 6 weeks in the PCB 126. The TEF compared PCB169 with PCB126, and distinctly increase of the C3 spot was observed for 15 weeks though the TEF was low. From these, as for the PCB 169, it was suggested appearing remarkably in aging influence of the immunity toxicity. The observations of the changes in these spots led to the conclusion that the changes in these spots resulted from transfer of the drugs accumulating in the maternal body to the F2 rats of the maternal rats administered PCB 126 and those administered PCB 169 via the breast milk and that these changes are involved with inflammatory proteins, including the target genes influenced by the toxicity of coplanar PCBs.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"67 1","pages":"25-31"},"PeriodicalIF":0.0,"publicationDate":"2006-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83255791","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

Mechanism of IgA-albumin complex formation that affects the fructosamine assay 影响果糖胺测定的iga -白蛋白复合物形成机制

Journal of capillary electrophoresis Pub Date : 2006-06-01 DOI: 10.2198/JELECTROPH.50.19

K. Fujita, F. Kameko, Y. Kato, M. Fukushima, N. Okumura, F. Terasawa, M. Sugano, K. Yamauchi, Hirohisa Sato, M. Kameko, I. Sakurabayashi

{"title":"Mechanism of IgA-albumin complex formation that affects the fructosamine assay","authors":"K. Fujita, F. Kameko, Y. Kato, M. Fukushima, N. Okumura, F. Terasawa, M. Sugano, K. Yamauchi, Hirohisa Sato, M. Kameko, I. Sakurabayashi","doi":"10.2198/JELECTROPH.50.19","DOIUrl":"https://doi.org/10.2198/JELECTROPH.50.19","url":null,"abstract":"We recently demonstrated glycation of monoclonal IgA and the presence of IgA-albumin complexes, but the mechanism of IgA-albumin complex formation was not clear. We isolated the IgA-albumin complexes from 5 IgA type M-proteinemia patients’ sera. To elucidate the mechanism of IgA-albumin complex formation, we performed the dissociation assay of IgA-albumin complexes, the identification of albumin binding sites of monoclonal IgA using immunoelectrophoresis, western blotting and chromatography technologies. In all patients with IgA type M-proteinemia, the IgA-albumin complexes were dissociated by treated with 2-mercaptoethanol (2-ME), but not by treated with a strong acid as acetic acid or NaCl of high concentrations. Moreover, when the purified monoclonal IgA containing IgA-albumin complexes was digested with the IgA protease from Neisseria gonorrhoeae, no macro-albumin was demonstrated. It seems probable that albumin is bound to the monoclonal IgA molecule by covalent disulfide bonds, and that the binding site of albumin is located in near the hinge region of IgA molecule and involve the free SH group thought to be present in the α-chain.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"269 1","pages":"19-23"},"PeriodicalIF":0.0,"publicationDate":"2006-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76953389","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

Comparative 2-DE proteomic analysis clarified that the stability of ITIH-4 is decreased under the storage at 4°C 对比2-DE蛋白质组学分析表明，ith -4在4°C的保存下稳定性下降

Journal of capillary electrophoresis Pub Date : 2006-06-01 DOI: 10.2198/JELECTROPH.50.13

Xiulian Zhang, Y. Kuramitsu, M. Fujimoto, K. Nakamura

引用次数: 1

A silver staining procedure for proteins in agarose gels 琼脂糖凝胶中蛋白质的银染色方法

Journal of capillary electrophoresis Pub Date : 2006-03-01 DOI: 10.2198/JELECTROPH.50.1

K. Yokomizo, S. Maruya, N. Hiratsuka, K. Shiba

引用次数: 1

Cell therapy with bone marrow cell for liver cirrhosis 骨髓细胞治疗肝硬化

Journal of capillary electrophoresis Pub Date : 2006-01-01 DOI: 10.2198/JELECTROPH.50.7

I. Sakaida

引用次数: 2

Comparative proteomics of flotillin-rich Triton X-100-insoluble lipid raft fractions of mitochondria and synaptosome from mouse brain 小鼠脑线粒体和突触体中富含漂浮蛋白的Triton x -100不溶性脂筏组分的比较蛋白质组学研究

Journal of capillary electrophoresis Pub Date : 2005-12-01 DOI: 10.2198/JELECTROPH.49.77

Megumi Nakamura, Y. Sakurai, Yasuo Takeda, T. Toda

{"title":"Comparative proteomics of flotillin-rich Triton X-100-insoluble lipid raft fractions of mitochondria and synaptosome from mouse brain","authors":"Megumi Nakamura, Y. Sakurai, Yasuo Takeda, T. Toda","doi":"10.2198/JELECTROPH.49.77","DOIUrl":"https://doi.org/10.2198/JELECTROPH.49.77","url":null,"abstract":"There is increasing evidence that lipid rafts may play important roles in brain neuronal cell functions including signal transduction. Meanwhile, the results suggesting possible presence of rafts in intracellular organelles such as mitochondria have been also reported. In this study, we compared proteins in raft-like structure of mitochondria to those of synaptosomal rafts and analyzed age-related alterations in protein in both mitochondrial and synaptosomal lipid rafts. A low density Triton X-100-insoluble fraction was prepared from cerebral cortical synaptosome and mitochondria of mouse and analyzed by two-dimensional (2-D) gel electrophoresis in combination with mass spectrometry. Co-localization of flotillin and cholesterol in Triton X-100-insoluble fraction of mitochondria was shown by Western blot analysis. Differential display of proteins using computer-aided image analysis revealed that the composition of protein in flotillin-rich Triton X-100-insoluble fraction of mitochondria was similar to that found in synaptosome. Several protein spots on 2-D gels varied in quantity depending on the age of the mouse, including the guanine nucleotide-binding protein G(O) alpha subunit, as identified by peptide mass fingerprinting.","PeriodicalId":15059,"journal":{"name":"Journal of capillary electrophoresis","volume":"3 1","pages":"77-83"},"PeriodicalIF":0.0,"publicationDate":"2005-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75113716","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: 7