Peter R. Jungblut

Max Planck Institute for Infection Biology

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Blanca Lapizco‐Encinas

Rochester Institute of Technology

Alejandro Cifuentes

Instituto de Investigación en Ciencias de la Alimentación

Bruce McCord

Florida International University

František Foret

Czech Academy of Sciences, Institute of Analytical Chemistry

Prashanta Dutta

Washington State University

P Kutter

Pohang TechnoPark (South Korea)

Bohuslav Gaš

Charles University

Brno

Pohang TechnoPark (South Korea)

Andreas Rizzi

University of Vienna

JÖ

J Örg

Pohang TechnoPark (South Korea)

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Charité - Universitätsmedizin Berlin

140

Max Planck Institute for Infection Biology

111

Max Planck Society

Humboldt-Universität zu Berlin

Center for Systems Biology

Digital Proteomics (United States)

Freie Universität Berlin

Centre National de la Recherche Scientifique

Inserm

Ludwig-Maximilians-Universität München

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Innovating the Concept and Practice of Two-Dimensional Gel Electrophoresis in the Analysis of Proteomes at the Proteoform Level

Xianquan Zhan Biao Li Xianquan Zhan Hartmut Schlüter Peter R. Jungblut

After several attempts to improve protein resolution by combining different electrophoretic methods, in 1975, O'Farrell published the combination of isoelectric focusing using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This combination resulted in a breakthrough in resolution where about 1000 spots could be resolved in one gel. This combination was named two-dimensional gel electrophoresis (2DE). Until quite recently, 2DE has largely been used to resolve and array proteins according to their isoelectric points and relative masses. Generally, a 2DE spot is a visible dot in a 2DE map, which is generated by 2DE-resolved proteoforms at a certain location. A spot is most generally visualized using stains, such as Coomassie or silver, or using fluorescent stains, such as Sypro Ruby and Flamingo. Every protein staining method has its own sensitivity. Spot detection thus correlates directly with the total amount of proteoforms present and the optical density of a spot does not give any information about the amount of any of the single components.

Proteome

10.1201/9781003298038-15

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Citations (1)

ChemInform Abstract: Back to the Future - The Value of Single Protein Species Investigations

ChemInform (2014)

Peter R. Jungblut

Abstract Review: 21 refs.

Value (mathematics)

10.1002/chin.201428285

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Citations (0)

Matrix-assisted laser desorption–ionization mass spectrometry peptide mass fingerprinting for proteome analysis: identification efficiency after on-blot or in-gel digestion with and without desalting procedures

Journal of Chromatography B Biomedical Sciences and Applications (2001)

Stephanie Lamer Peter R. Jungblut

Peptide mass fingerprinting

Bottom-up proteomics

Proteome

Coomassie Brilliant Blue

Digestion

10.1016/s0378-4347(00)00446-1

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Citations (42)

Famose Kerle : Eulenburg : eine wilhelminische Affäre

Peter R. Jungblut

Source

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Citations (2)

Editorial Board: Electrophoresis 22-23'17

Electrophoresis (2017)

Ziad El Rassi Stillwater Franti Šek Foret Andreas Rizzi Nancy C. Stellwagen

10.1002/elps.201770182

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Citations (0)

Editorial Board: Electrophoresis 15'12

Electrophoresis (2012)

Ziad El Rassi Stillwater Petr Bo Brno Andreas Rizzi

Editorial board

10.1002/elps.201270102

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Citations (0)

Editorial Board: Electrophoresis 21'18

Electrophoresis (2018)

Ziad El Rassi Stillwater Franti Šek Foret Yi Chen Alejandro Cifuentes

Editorial board

10.1002/elps.201870173

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Citations (0)

Peptide mass fingerprinting

Methods (2005)

Bernd Thiede Wolfgang Höhenwarter Alexander Krah Jens Mattow Monika Schmid

Peptide mass fingerprinting

10.1016/j.ymeth.2004.08.015

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Citations (275)

The analysis of S100A9 and S100A8 expression in matched sets of macroscopically normal colon mucosa and colorectal carcinoma: The S100A9 and S100A8 positive cells underlie and invade tumor mass

Electrophoresis (1999)

Jiří Stulík Jan Österreicher Kamila Koupilová Jiří Knížek Aleš Macela

The expression of calcium-binding protein S100A9 was investigated in 23 matched sets of colorectal carcinoma and normal colon mucosa using two-dimensional gel electrophoresis. We found that, from a group of 23 patients, the level of S100A9 protein, in comparison with matched normal colon mucosa, was significantly increased in malignant tissues of 16 patients (70%). Furthermore, an additional protein, identified by matrix-assisted laser desorption/ionization - mass spectrometry (MALDI-MS) as S100A8, exhibited an increased expression in the same specimens of malignant tissues as the S100A9 protein. The immunohistological analysis revealed the accumulation of S100A9 positive cells, macrophages and polymorphonuclear leukocytes along the invasive margin of colorectal carcinoma. The S100A8 protein was found to be produced in the same location. The possible participation of both proteins and, especially, its heterodimeric complex calprotectin in colorectal carcinoma regression could be taken into account.

S100A9

S100A8

S100 protein

10.1002/(sici)1522-2683(19990101)20:4/5<1047::aid-elps1047>3.0.co;2-e

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Citations (100)

Identification and characterization of heat shock protein 27 protein species in human myocardial two‐dimensional electrophoresis patterns

Electrophoresis (1997)

Christian Scheler Eva‐Christina Müller Joachim Stahl Ursula Müller‐Werdan Johann Salnikow

Abstract Immunostaining of heat shock protein 27 (Hsp27) protein species on two‐dimensional electrophoresis (2‐DE) gels with enhanced sensitivity yields 59 spots reacting with anti‐Hsp27 antibodies. Recombinant Hsp27 exists in 2‐DE as two major protein species which comigrate in the human myocardial pattern with Hsp27 spots C754 and D899 as defined in the heart high‐performance 2‐DE database ( http://www.mdc‐berlin.de/∼emu/heart/ ). Preparative electrophoresis of human myocardial proteins and analysis of the enriched mass range 20–30 kDa by 2‐DE revealed eight protein spots (C438, C582, C658, C697, C754, C595, C750) from the human myocardial database and a new spot not previously detected on silver‐stained gels. These spots were identified as Hsp27 protein species by enzymatic in‐gel‐digestion and analysis by matrix assisted laser desorption‐ionization (MALDI) peptide mass fingerprinting and, in part, MALDI‐post source decay sequencing of single fragments. Possible post‐translational modifications were investigated: immunostaining tests with anti‐phospho‐serine/‐threonine/‐tyrosine antibodies, although positive for other myocardial proteins, were negative for presumed Hsp27 protein species; likewise, periodate‐glycostaining assays and biotinylation screening did not detect modifications in the investigated Hsp27 protein species.

Peptide mass fingerprinting

Hsp27

Immunostaining

Proteome

10.1002/elps.1150181518

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Citations (63)