Identification of Thymosin Proteins in Human Bladder Tumor Cells by Mass Spectrometry and Data Base Searching
スポンサーリンク
概要
- 論文の詳細を見る
A study of the induction of metallothionein isoforms in human T24 bladder tumor cells revealed the presence of coeluting unknown proteins that were also heat stable and had molecular masses in the same range. In order to determine any relationship to metallothionein isoforms, these unknown proteins were identified, using database searching based on mass spectrometric determination of molecular weights, tryptic peptide mass maps and partial sequences. This study demonstrates that heat stable thymosin β-4 and β-10 are expressed in human bladder tumor cells.
- 日本質量分析学会の論文
- 1998-02-01
著者
-
Fabris Daniele
Department Of Chemistry And Biochemistry Structural Biochemistry Center University Of Maryland Balti
-
HE Tao
Department of Chemistry and Biochemistry, Structural Biochemistry Center, University of Maryland Bal
-
FENSELAU Catherine
Department of Chemistry and Biochemistry, Structural Biochemistry Center, University of Maryland Bal
-
He Tao
Department Of Chemistry And Biochemistry Structural Biochemistry Center University Of Maryland Balti
-
Fenselau Catherine
Department Of Chemistry & Biochemistry And Marlene & Stewart Greenebaum Cancer Center Univer
-
Fenselau Catherine
Department Of Chemistry And Biochemistry Structural Biochemistry Center University Of Maryland Balti
関連論文
- Identification of Thymosin Proteins in Human Bladder Tumor Cells by Mass Spectrometry and Data Base Searching
- Controlled/"Living" Radical Ring-Opening Polymerization of 5, 6-Benzo-2-Methylene-1, 3-Dioxepane Based on Reversible Addition-Fragmentation Chain Transfer Mechanism
- Intercharge Distances in Zn_7-Metallothionein Analyzed by Nanospray on a Quadrupole Ion Trap and Molecular Modeling
- A review of quantitative methods for proteomic studies
- Evaluation of Solution Phase Isoelectrofocusing as Part of Proteomics Strategies