TAILIEUCHUNG - Báo cáo khoa học: Proteome analysis of a rat liver nuclear insoluble protein fraction and localization of a novel protein, ISP36, to compartments in the interchromatin space

A rat liver nuclear insoluble protein fraction was analyzed to investigate candidate proteins participating in nuclear architecture formation. Proteins were subjected to two-dimensional separation by reversed-phase HPLC in 60% formic acid and SDS⁄PAGE. The method produced good resolution of insoluble proteins. One hundred and thirty-eight proteins were separ-ated, and 28 of these were identified. | ềFEBS Journal Proteome analysis of a rat liver nuclear insoluble protein fraction and localization of a novel protein ISP36 to compartments in the interchromatin space Masashi Segawa1 Koko Niino1 Reiko Mineki2 Naoko Kaga2 Kimie Murayama2 Kenji Sugimoto3 Yuichi Watanabe4 Kazuhiro Furukawa1 5 and Tsuneyoshi Horigome1 5 6 1 NaturalScience Course Graduate Schoolof Science and Technology Niigata University Japan 2 Division of Proteomics and Biomolecular Science BiomedicalResearch Center Juntendo University Graduate Schoolof Medicine Tokyo Japan 3 Division of Applied Biochemistry Graduate Schoolof Agriculture and BiologicalSciences Osaka Prefecture University Japan 4 Department of Biology Niigata University Japan 5 Department of Chemistry Niigata University Japan 6 Center for Transdisciplinary Research Niigata University Japan Keywords ISP36 interchromatin space protein nuclear matrix protein nuclear protein proteome insoluble protein proteome Correspondence T. Horigome Department of Chemistry Faculty of Science Niigata University Igarashi-2 Niigata 950-2181 Japan Fax 81 25 262 6160 Tel 81 25 262 6160 E-mail thori@ Received 27 March 2005 revised 4 July 2005 accepted 5 July 2005 doi A rat liver nuclear insoluble protein fraction was analyzed to investigate candidate proteins participating in nuclear architecture formation. Proteins were subjected to two-dimensional separation by reversed-phase HPLC in 60 formic acid and SDS PAGE. The method produced good resolution of insoluble proteins. One hundred and thirty-eight proteins were separated and 28 of these were identified. The identified proteins included one novel protein seven known nuclear proteins and 12 known nuclear matrix proteins. The novel 36 kDa protein was further investigated for its sub-nuclear localization. The human ortholog of the protein was expressed in Escherichia coli and antibodies were raised against the recombinant protein. Exclusive .

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