A two-dimensional gel database of human plasma proteins

Area of Science:

• Proteomics
• Biochemistry
• Human Physiology

Background:

• Human plasma proteome complexity presents challenges for comprehensive analysis.
• Accurate protein mapping is crucial for understanding biological functions and disease states.

Purpose of the Study:

• To provide an updated and detailed two-dimensional electrophoretic map of human plasma proteins.
• To catalog identified protein species, their locations, sizes, and isoelectric points.
• To highlight previously uncharacterized proteins within the plasma proteome.

Main Methods:

• Utilized two-dimensional electrophoresis (2-DE) for high-resolution separation of human plasma proteins.
• Characterized protein spots based on location, molecular weight, and isoelectric point (pI).
• Compared and updated existing protein maps with new data.

Main Results:

• An updated 2-DE map of human plasma proteins was successfully generated.
• Forty-nine distinct polypeptide species were identified and cataloged.
• Multiple spots for certain proteins (e.g., immunoglobulins) indicated variations in glycosylation or sequence.
• An additional 35 uncharacterized proteins were detected, suggesting further complexity.

Conclusions:

• The updated map provides a valuable resource for human plasma proteomics research.
• The identification of numerous protein variants and uncharacterized proteins opens avenues for further investigation.
• This detailed protein atlas aids in the discovery of biomarkers and understanding of plasma protein function.