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Human migration inhibitory factor: purification and immunochemical characterization

L H Block, H Jaksche, S Bamberger

The Journal of Experimental Medicine

|February 1, 1978

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Migration inhibitory factor (MIF) from human lymphocytes was purified and characterized. This acidic protein, approximately 25,000 daltons, inhibits macrophage migration and electrophoretic mobility, with specific antibodies neutralizing its effects.

Area of Science:

Immunology
Protein Biochemistry

Background:

Macrophage migration is crucial in immune responses.
Lymphocyte activation leads to the release of signaling molecules.

Purpose of the Study:

To highly purify and characterize the migration inhibitory factor (MIF) from activated human lymphocytes.
To investigate the biological functions and immunological properties of purified MIF.

Main Methods:

Gel filtration chromatography
Preparative isotachophoresis
Analytical polyacrylamide gel electrophoresis (SDS-PAGE)
Capillary migration inhibition test
Macrophage electrophoretic mobility assay
Immunochemical techniques (antibody production and neutralization assays)

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Main Results:

MIF was successfully purified from concanavalin A-activated human lymphocytes.
Purified MIF is an acidic protein with an approximate molecular weight of 25,000 daltons.
MIF inhibited macrophage migration in the capillary test and reduced macrophage electrophoretic mobility.
Specific rabbit antibodies against MIF neutralized its biological activities.

Conclusions:

The purified protein is identified as migration inhibitory factor (MIF).
MIF plays a significant role in modulating macrophage behavior, specifically migration and mobility.
Immunological neutralization confirms the specificity and biological relevance of MIF.