Reducing Sample Complexity in Proteomics by Chromatofocusing with Simple Buffer Mixtures

Shen, Hong; Li, Xiang; Bieberich, Charles J.; Frey, Douglas D.

doi:10.1007/978-1-60327-064-9_16

Cited by 11 publications

(4 citation statements)

References 17 publications

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“…The mini Rotofor contains 18 mL of separation volume as compared to the larger device. It is important to note that, while the technique is not carrier ampholyte nor electrophoretic-based, chromatofocusing is another analytical method in which proteins or other ampholytes can be separated according to isoelectric point [32,33]. Typically, chromatofocusing utilizes ion exchange resins and changes in buffer pH to separate species according to their isoelectric point.…”

Section: 2de and Ipg Stripsmentioning

confidence: 99%

Isoelectric Point Separations of Peptides and Proteins

Pergande

Cologna

2017

Proteomes

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The separation of ampholytic components according to isoelectric point has played an important role in isolating, reducing complexity and improving peptide and protein detection. This brief review outlines the basics of isoelectric focusing, including a summary of the historical achievements and considerations in experimental design. Derivative methodologies of isoelectric focusing are also discussed including common detection methods used. Applications in a variety of fields using isoelectric point based separations are provided as well as an outlook on the field for future studies.

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Section: 2de and Ipg Stripsmentioning

confidence: 99%

Isoelectric Point Separations of Peptides and Proteins

Pergande

Cologna

2017

Proteomes

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“…The complexity of protein samples has always been a major obstacle of proteomic study (Hondermarck, 2003;Speicher, 2007;Shen et al, 2008). Larvae and adults of many marine invertebrates are protected by shell (e.g., B. amphitrite), calcareous tubes (H. elegans), and mucilaginous polysaccharide substances (P. vexillosa and C. teleta).…”

Section: Challenges and Future Directions Sample Preparationmentioning

confidence: 99%

Proteomics insights: proteins related to larval attachment and metamorphosis of marine invertebrates

2014

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The transition in an animal from a pelagic larval stage to a sessile benthic juvenile typically requires major morphological and behavioral changes. Larval competency, attachment and initiation of metamorphosis are thought to be regulated by intrinsic chemical signals and specific sets of proteins. However, the molecular mechanisms that regulate larval attachment and metamorphosis in marine invertebrates have yet to be fully elucidated. Despite the many challenges associated with analysis of the larvae proteome, recent proteomic technologies have been used to address specific questions in larval developmental biology. These and other molecular studies have generated substantial amount of information of the proteins and molecular pathways involved in larval attachment and metamorphosis. Furthermore, the results of these studies have shown that systematic changes in protein expression patterns and post-translational modifications (PTMs) are crucial for the transition from larva to juvenile. The degeneration of larval tissues is mediated by protein degradation, while the development of juvenile organs may require PTM. In terms of application, the identified proteins may serve as targets for antifouling compounds, and biomarkers for environmental stressors. In this review we highlight the strengths and limitations of proteomic tools in the context of the study of marine invertebrate larval biology.

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“…As with gel-based methods, the combination of different analytical strategies such as in multi-dimensional LC (nDLC) increases resolution 59-62 . The separation of peptides by two-dimensional LC (2DLC) after protein digestion is referred to as shotgun approach 63, 64 , as opposed to 2DLC systems that separate intact proteins, potentially providing additional information about protein isoforms and PTM status 65-67 .…”

Section: Protein and Peptide Separation Techniquesmentioning

confidence: 99%

Divide and Conquer

Agnetti

Husberg

Eyk

2011

Circulation Research

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Chronic heart failure is a worldwide cause of mortality and morbidity and is the final outcome of a number of different etiologies. This reflects both the complexity of the disease and our incomplete understanding of its underlying molecular mechanisms. One experimental approach to address this is to study subcellular organelles and how their functions are activated and synchronized under physiological and pathological conditions. In this review, we discuss the application of proteomic technologies to organelles and how this has deepened our perception of the cellular proteome and its alterations with heart failure. The use of proteomics to monitor protein quantity and post-translational modifications (PTMs) has revealed a highly intricate and sophisticated level of protein regulation. PTMs have the potential to regulate organelle function and interplay most likely by targeting both structural and signaling proteins throughout the cell, ultimately coordinating their responses. The potentials and limitations of current proteomic technologies are also discussed emphasizing that the development of novel methods will enhance our ability to further investigate organelles and decode intracellular communication.

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Reducing Sample Complexity in Proteomics by Chromatofocusing with Simple Buffer Mixtures

Cited by 11 publications

References 17 publications

Isoelectric Point Separations of Peptides and Proteins

Isoelectric Point Separations of Peptides and Proteins

Proteomics insights: proteins related to larval attachment and metamorphosis of marine invertebrates

Divide and Conquer

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