Blood plasma fractionation

Source: Wikipedia, the free encyclopedia.

Blood plasma

autoimmune inflammatory
diseases.

Blood plasma

platelets
are suspended within the plasma.

Plasma proteins

Plasma contains a large variety of proteins including

disulfide bonds and unique in that it has the highest water solubility and the lowest isoelectric point (pI) of the plasma proteins. Due to the structural integrity of albumin it remains stable under conditions where most other proteins denature
.

Plasma proteins for clinical use

Many of the proteins in plasma have important therapeutic uses.

plasma exchange.[3] Since albumin is the most abundant protein in the plasma its use may be the most well known, but many other proteins, although present in low concentrations, can have important clinical uses.[1] See table below.[1]

Examples of Plasma Components for Clinical Use
Plasma Component Reasons for Use
factor VIII
hemophilia A
factor IX
hemophilia B
Factor X congenital deficiency
factor XIII congenital deficiency
PCC complex
overdose

deficiencies liver disease

immunoglobulin
passive prophylaxis

immune deficiency
disorders
some types of immune thrombocytopenic purpura
Guillain–Barré syndrome
Polyneuropathies

antithrombin III
congenital deficiency

disseminated intravascular coagulation

fibrinogen congenital deficiency

massive

haemorrhage

C1 inhibitor
hereditary angioedema
albumin hypoalbuminemia

Ascites Restoring of blood volume in trauma, burns and surgery patients

alpha-I-antitrypsin
hereditary deficiencies

emphysema and COPD cirrhosis

Plasma processing

When the ultimate goal of plasma processing is a purified plasma component for

precipitate is purified albumin. Several variations to this process exist, including an adapted method by Nitschmann and Kistler that uses fewer steps and replaces centrifugation and bulk freezing with filtration and diafiltration.[1][3]

Some newer methods of albumin purification add additional purification steps to the Cohn Process and its variations, while others incorporate

ion exchange chromatography steps.[3] After ion exchange there are generally further chromatographic purification steps and buffer exchange.[3]

For further information see chromatography in blood processing.

Plasma for analytical uses

In addition to the clinical uses of a variety of plasma proteins, plasma has many analytical uses. Plasma contains many

diseases, and separation of plasma is a necessary step in the expansion of the human plasma proteome
.

Plasma in clinical diagnosis

Plasma contains an abundance of proteins many of which can be used as biomarkers, indicating the presence of certain diseases in an individual. Currently, 2D Electrophoresis is the primary method for discovery and detection of biomarkers in plasma. This involves the separation of plasma proteins on a gel by exploiting differences in their size and pI. Potential disease biomarkers may be present in plasma at very low concentrations, so, plasma samples must undergo preparation procedures for accurate results to be obtained using 2D Electrophoresis. These preparation procedures aim to remove contaminants that may interfere with detection of biomarkers, solubilize the proteins so they are able to undergo 2D Electrophoresis analysis, and prepare plasma with minimal loss of low concentration proteins, but optimal removal of high abundance proteins.

The future of laboratory diagnostics are headed toward lab-on-a-chip technology, which will bring the laboratory to the point-of-care. This involves integration of all of the steps in the analytical process, from the initial removal of plasma from whole blood to the final analytical result, on a small microfluidic device. This is advantageous because it reduces turn around time, allows for the control of variables by automation, and removes the labor-intensive and sample wasting steps in current diagnostic processes.

Expansion of the human plasma proteome

The human plasma proteome may contain thousands of proteins, however, identifying them presents challenges due to the wide range of concentrations present. Some low abundance proteins may be present in

cation exchange chromatography and subsequent tandem mass spectrometry for protein identification.[2][4]

See also

References

  1. ^ a b c d e Brodniewicz-Proba, T. 1991. "Human Plasma Fractionation and the Impact of New Technologies on the Use and Quality of Plasma-derived Products". Blood Reviews. Vol. 5. pp.245-257.
  2. ^ a b Shen, Y., Jacobs, J. M., et al. 2004. "Ultra-High-Efficiency Strong Cation Exchange LC/RPLC/MS/MS for High Dynamic Range Characterization of the Human Plasma Proteome". Anal Chem. Vol. 76. pp. 1134-1144.
  3. ^ a b c d e f g h i Matejtschuk, P., Dash, C.H., and Gascoigne, E.W. 2000. "Production of human albumin solution: a continually developing colloid". British Journal of Anaesthesia. Vol 85. pp. 887-895.
  4. ^ Wu, S., Choudhary, G., et al. 2003. ""Evaluation of Shotgun Sequencing for Proteomic Analysis of Human Plasma Using HPLC coupled with Either Ion Trap or Fourier Transform Mass Spectrometry"". Journal of Proteome Research. Vol. 2. pp. 383-393.