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Composition of Blood Plasma01:24

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Blood plasma is a fluid that contains approximately 92% water and 8% solutes. The solutes include various types of proteins, which constitute about 7% of the total solutes in the plasma. The high-molecular-weight proteins—albumins, globulins, and fibrinogen—are essential to plasma function. Albumins, making up about 60% of the plasma proteins, maintain the osmotic balance within blood vessels by preventing excessive water leakage. Additionally, albumins serve as carrier proteins,...
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Cell division and enlargement are processes that require precise control. The control ensures that cell division cannot proceed unless the cell has grown to a specific size. A spherical, dividing cell requires an approximately 1.6X increase in its surface area to double its volume. The secretory pathway also has a significant role in cell membrane enlargement. Secretory vesicles that bud off from the Golgi apparatus and later fuse with the plasma membrane during exocytosis are a major source of...
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Updated: Feb 1, 2026

Basic Research in Plasma Medicine - A Throughput Approach from Liquids to Cells
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The plasma peptidome.

Jaimie Dufresne1, Pete Bowden1, Thanusi Thavarajah1

  • 11Ryerson Analytical Biochemistry Laboratory (RABL), Department of Chemistry and Biology, Faculty of Science, Ryerson University, 350 Victoria St, Toronto, ON Canada.

Clinical Proteomics
|December 7, 2018
PubMed
Summary

This study developed a method to analyze the plasma proteome, identifying over 14,000 gene symbols. This approach allows for the discovery of clinically significant protein variations across different patient populations.

Keywords:
Electrospray ionization tandem mass spectrometryEndogenous tryptic peptides phospho peptidesHuman EDTA plasmaLC–ESI–MS/MSLinear quadrupole ion trapNano chromatographyOrganic extraction

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Area of Science:

  • Proteomics
  • Biochemistry
  • Clinical Chemistry

Background:

  • Discovering novel diagnostic or therapeutic peptides/proteins from blood plasma is crucial.
  • Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) coupled with a linear quadrupole ion trap enables peptide identification, quantification, and statistical comparison.
  • Ex vivo cleavage of plasma peptides offers a pathway to analyze protein distributions across diverse clinical populations.

Purpose of the Study:

  • To establish a systematic method for organic fractionation of plasma peptides.
  • To identify and quantify endogenous tryptic peptides from human plasma using advanced mass spectrometry techniques.
  • To compare statistical distributions of peptides across different clinical populations for potential diagnostic or therapeutic insights.

Main Methods:

  • Applied a systematic organic fractionation method to human plasma peptides.
  • Utilized C18 High-Performance Liquid Chromatography (HPLC) followed by nano electrospray ionization and tandem mass spectrometry (LC-ESI-MS/MS).
  • Analyzed tryptic peptides from 6 institutions, 12 disease/normal plasma populations, and controls using mass spectrometry and SQL Server R for data analysis.

Main Results:

  • Identified and quantified approximately 14,000 gene symbols, representing the largest number of blood proteins identified to date.
  • Demonstrated the ability to monitor ex vivo proteolysis of most human proteins, including interleukins.
  • Over 1.9 million distinct peptide correlations were analyzed, with algorithms like SEQUEST and X!TANDEM identifying thousands of protein accessions and gene symbols with high confidence.

Conclusions:

  • The developed LC-ESI-MS/MS method with SQL Server-R analysis revealed the largest plasma proteome to date.
  • This practical method allows quantification and comparison of ex vivo cleaved proteins across populations, facilitating the discovery of treatment-specific variations.
  • Nearly all human proteins from EDTA plasma were identified and quantified, enabling comparisons across multiple clinical populations using standard database and statistical methods.