High resolution two-dimensional electrophoresis of proteins.

O’Farrell, Patrick H.

doi:10.1016/s0021-9258(19)41496-8

Cited by 18,117 publications

(1,347 citation statements)

References 34 publications

Supporting

Mentioning

1,313

Contrasting

Unclassified

Order By: Relevance

“…One-third of each translation assay was analyzed on a twodimensional polyacrylamide gel as described by O'Farrell (27). The lysis buffer was modified to contain 0.1% sodium dodecyl sulfate (6).…”

Section: Methodsmentioning

confidence: 99%

Drosophila melanogaster has only one myosin alkali light-chain gene which encodes a protein with considerable amino acid sequence homology to chicken myosin alkali light chains

et al. 1984

View full text Add to dashboard Cite

A chimeric lambda DNA molecule containing the myosin alkali light-chain gene of Drosophila melanogaster was isolated. The encoded amino acid sequence was determined from the nucleic acid sequence of a cDNA homologous to the genomic clone. The identity of the encoded protein was established by two criteria: (i) sequence homology with the chicken alkali light-chain proteins and (ii) comparison of the two-dimensional gel electrophoretic pattern of the peptides synthesized by in vitro translation of hybrid-selected RNA to that of myosin alkali light-chain peptides extracted from Drosophila myofibrils. There is only one myosin alkali light-chain in D. melanogaster; its chromosomal location is region 98B . This gene is abundantly expressed during the development of larval as well as adult muscles. The Drosophila protein appears to contain one putative divalent cation-binding domain (an EF hand) as compared with the three EF hands present in chicken alkali light chains.

show abstract

Section: Methodsmentioning

confidence: 99%

Drosophila melanogaster has only one myosin alkali light-chain gene which encodes a protein with considerable amino acid sequence homology to chicken myosin alkali light chains

et al. 1984

View full text Add to dashboard Cite

show abstract

“…Two decades ago, the term platelet proteomics was mainly referred to two-dimensional gel electrophoresis (2-DE), where the proteins are separated according to their isoelectric point in the first and by molecular weight in the second dimension [ 66 , 67 , 68 ]. This technology was used to identify proteins and mapping protein phosphorylation of rested and activated platelets, the composition of platelets subcellular organelles, e.g., lipid rafts, membrane, secreted granules, and platelet microparticles [ 69 , 70 , 71 , 72 , 73 ].…”

Section: Platelets Proteomicsmentioning

confidence: 99%

Proteomics: A Tool to Study Platelet Function

Shevchuk

Begonja

Gambaryan

et al. 2021

IJMS

View full text Add to dashboard Cite

Platelets are components of the blood that are highly reactive, and they quickly respond to multiple physiological and pathophysiological processes. In the last decade, it became clear that platelets are the key components of circulation, linking hemostasis, innate, and acquired immunity. Protein composition, localization, and activity are crucial for platelet function and regulation. The current state of mass spectrometry-based proteomics has tremendous potential to identify and quantify thousands of proteins from a minimal amount of material, unravel multiple post-translational modifications, and monitor platelet activity during drug treatments. This review focuses on the role of proteomics in understanding the molecular basics of the classical and newly emerging functions of platelets. including the recently described role of platelets in immunology and the development of COVID-19.The state-of-the-art proteomic technologies and their application in studying platelet biogenesis, signaling, and storage are described, and the potential of newly appeared trapped ion mobility spectrometry (TIMS) is highlighted. Additionally, implementing proteomic methods in platelet transfusion medicine, and as a diagnostic and prognostic tool, is discussed.

show abstract

“…It was also very appropriate that the proteome concept emerged from the 2D gel electrophoresis international research community, a group that engages and develops high resolution protein separation technologies using gel electrophoresis and chromatography. In 1975, 2D gel electrophoresis of proteins, first by charge using isoelectric focusing (IEF) and then by mass using SDS PAGE, was first reported by 3 groups mapping proteins from organisms as diverse as Escherichia coli, mouse, and guinea pig, respectively (Klose, 1975;O'Farrell, 1975;Scheele, 1975). For more than 2 decades, proteins could not be readily identified from 2D gels, even with the introduction of automated protein sequencers (Celis et al, 1989), until linkage of this separation technology with mass spectrometry in the mid 1990s (Yates, 2004).…”

Section: Evolution Of Proteomicsmentioning

confidence: 99%

“…Two-dimensional polyacrylamide gel electrophoresis (2D PAGE) is a frequently used proteomics method in protein separation that can resolve complex protein mixtures by charge by isoelectric focusing and by mass using SDS PAGE electrophoresis (O'Farrell, 1975). Resolved proteins are visualized with colored stains including colloidal Coomassie blue, silver, and gold, or more recently by sensitive fluorescent dyes such as Sypro ruby (Lauber et al, 2001).…”

Section: Two-dimensional Polyacrylamide Gel Electrophoresis and Mass Spectrometrymentioning

confidence: 99%

Invited Review: Toxicoproteomics: Proteomics Applied to Toxicology and Pathology

2004

View full text Add to dashboard Cite

Global measurement of proteins and their many attributes in tissues and biofluids defines the field of proteomics. Toxicoproteomics, as part of the larger field of toxicogenomics, seeks to identify critical proteins and pathways in biological systems that are affected by and respond to adverse chemical and environmental exposures using global protein expression technologies. Toxicoproteomics integrates 3 disciplinary areas: traditional toxicology and pathology, differential protein and gene expression analysis, and systems biology. Key topics to be reviewed are the evolution of proteomics, proteomic technology platforms and their capabilities with exemplary studies from biology and medicine, a review of over 50 recent studies applying proteomic analysis to toxicological research, and the recent development of databases designed to integrate -Omics technologies with toxicology and pathology. Proteomics is examined for its potential in discovery of new biomarkers and toxicity signatures, in mapping serum, plasma, and other biofluid proteomes, and in parallel proteomic and transcriptomic studies. The new field of toxicoproteomics is uniquely positioned toward an expanded understanding of protein expression during toxicity and environmental disease for the advancement of public health.

show abstract

High resolution two-dimensional electrophoresis of proteins.

Cited by 18,117 publications

References 34 publications

Drosophila melanogaster has only one myosin alkali light-chain gene which encodes a protein with considerable amino acid sequence homology to chicken myosin alkali light chains

Drosophila melanogaster has only one myosin alkali light-chain gene which encodes a protein with considerable amino acid sequence homology to chicken myosin alkali light chains

Proteomics: A Tool to Study Platelet Function

Invited Review: Toxicoproteomics: Proteomics Applied to Toxicology and Pathology

Contact Info

Product

Resources

About