A5087840752- Advanced Proteomics Techniques and Applications
- Mass Spectrometry Techniques and Applications
- Metabolomics and Mass Spectrometry Studies
- Protein Structure and Dynamics
- Biosensors and Analytical Detection
- Monoclonal and Polyclonal Antibodies Research
- Advanced Biosensing Techniques and Applications
- Protein purification and stability
- Glycosylation and Glycoproteins Research
- Machine Learning in Bioinformatics
- Molecular Biology Techniques and Applications
- SARS-CoV-2 detection and testing
- Gene expression and cancer classification
- Muscle Physiology and Disorders
- Viral Infectious Diseases and Gene Expression in Insects
- Pharmacogenetics and Drug Metabolism
- Liver Disease Diagnosis and Treatment
- Carcinogens and Genotoxicity Assessment
- Erythrocyte Function and Pathophysiology
- Genetics, Bioinformatics, and Biomedical Research
- Enzyme Structure and Function
- Microbial Metabolic Engineering and Bioproduction
- Drug Transport and Resistance Mechanisms
- Advanced biosensing and bioanalysis techniques
- Bioinformatics and Genomic Networks
Mayo Clinic
2014
American Red Cross
2012
Proteome Sciences (United Kingdom)
2011
Food and Drug Administration
2009
University of Victoria
2004
Genome British Columbia
2004
Emory University
2002
Complete Genomics (United States)
2000-2001
Meso Scale Discovery (United States)
1991-2000
Research Triangle Park Foundation
1995
We have merged four different views of the human plasma proteome, based on methodologies, into a single nonredundant list 1175 distinct gene products. The methodologies used were 1) literature search for proteins reported to occur in or serum; 2) multidimensional chromatography followed by two-dimensional electrophoresis and mass spectroscopy (MS) identification resolved proteins; 3) tryptic digestion peptides MS identification; 4) from low-molecular-mass components identification. Of 1,175...
A method (denoted SISCAPA) for quantitation of peptides in complex digests is described. In the method, anti-peptide antibodies immobilized on 100 nanoliter nanoaffinity columns are used to enrich specific along with spiked stable-isotope-labeled internal standards same sequence. Upon elution from antibody supports, electrospray mass spectrometry quantitate (natural and labeled). a series pilot experiments, tryptic test were chosen four proteins human plasma (hemopexin, α1 antichymotrypsin,...
Plasma, the soluble component of human blood, is believed to harbor thousands distinct proteins, which originate from a variety cells and tissues through either active secretion or leakage blood tissues. The dynamic range plasma protein concentrations comprises at least nine orders magnitude. Proteins involved in coagulation, immune defense, small molecule transport, protease inhibition, many them present high abundance this body fluid, have been functionally characterized associated with...
Mass spectrometry-based multiple reaction monitoring (MRM) quantitation of proteins can dramatically impact the discovery and biomarkers via rapid, targeted, multiplexed protein expression profiling clinical samples. A mixture 45 peptide standards, easily adaptable to common plasma proteomics work flows, was created permit absolute endogenous in human trypsin digests. All experiments were performed on simple tryptic digests EDTA-plasma without prior affinity depletion or enrichment. Stable...
In order to discover novel protein markers indicative of disease processes or drug effects, the proteomics technology platform most commonly used consists high resolution separation by two-dimensional electrophoresis (2-DE), mass spectrometric identification proteins from stained gel spots and a bioinformatic data analysis process supported statistics. This approach has been more successful in profiling their disease- treatment-related quantitative changes tissue homogenates than plasma...
Vol. 1 (2002) 845–867The Human Plasma Proteome: History, Character, and Diagnostic ProspectsN. Leigh Anderson Norman G. AndersonPage 856, Fig. 3: The positions of proteins on the figure was incorrect. correct is shown following. N. Page
The inability to quantify large numbers of proteins in tissues and biofluids with high precision, sensitivity, throughput is a major bottleneck biomarker studies. We previously demonstrated that coupling immunoaffinity enrichment using anti-peptide antibodies (SISCAPA) multiple reaction monitoring mass spectrometry (MRM-MS) produces Immunoprecipitation MRM-MS (immuno-MRM-MS) assays can be multiplexed plasma specificity, precision. Here we report the first systematic evaluation...
A SISCAPA (stable isotope standards and capture by anti-peptide antibodies) method for specific antibody-based of individual tryptic peptides from a digest whole human plasma was developed using simplified magnetic bead protocol novel rotary trap device. Following off-line equilibrium binding antibodies subsequent the on beads, permitted washing beads elution bound inside 150-microm-inner diameter capillary that forms part nanoflow LC-MS/MS system. The sweeps against direction liquid flow...
Stable isotope standards and capture by antipeptide antibodies (SISCAPA) couples affinity enrichment of peptides with stable dilution detection multiple reaction monitoring mass spectrometry to provide quantitative measurement as surrogates for their respective proteins. In this report, we describe a feasibility study determine the success rate production suitable SISCAPA assays in order inform strategies large-scale assay development. A workflow was designed that included multiplex...
Abstract We have improved upon the reference two‐dimensional (2‐D) electrophoretic map of rat liver proteins originally published in 1991 (N. L. Anderson et al. , Electrophoresis 1991, 12 907–930). A total 53 (102 spots) are now identified, many by microsequencing. In most cases, spots cut from wet, Coomassie Blue stained 2‐D gels were submitted to internal tryptic digestion [2], and individual peptides, separated high‐performance liquid chromatography (HPLC), sequenced using a Perkin‐Elmer...
Abstract An updated two‐dimensional electrophoretic map of human plasma proteins is presented, together with a complete listing the individual protein spots, their locations, size and isoelectric points relative to internal charge standards. Forty‐nine polypeptide species are identified, many consisting multiple spots differing in glycosylation or sequence ( e.g. , immunoglobulins). A further series 35 as yet uncharacterized indicated.
Abstract A standard two‐dimensional (2‐D) protein map of Fischer 344 rat liver (F344MST3) is presented, with a tabular listing more than 1200 species. Sodium dodecyl sulfate (SDS) molecular mass and isoelectric point have been established, based on positions numerous internal standards. This has used to connect compare hundreds 2‐D gels samples from variety studies, forms the nucleus an expanding database describing proteins their regulation by various drugs toxic agents. An example such...
Abstract Human plasma proteins separated by high‐resolution two‐dimensional electrophoresis have been electrophoretically transferred to sheets of nitrocellulose using a modification the method Towbin, Staehelin, and Gordon [8]. Although denatured in sodium dodecyl sulfate into subunits, nitrocellulose‐bound molecules still react with appropriate specific antisera even after storage transfer air at room temperature for 5 months. Of 25 whose location pattern had previously determined, 24 are...