PMID: 7027252Jul 1, 1981Paper

Purification of guinea pig pH 3 migration inhibitory factor

Proceedings of the National Academy of Sciences of the United States of America
H G RemoldA D Mednis

Abstract

Macrophage migration inhibitory factor (MIF) from the guinea pig was recently shown to reside in two discrete and separable proteins referred to as pH 3 MIF and pH 5 MIF. One subfraction of pH 3 MIF has now been purified to apparent homogeneity from supernatants of stimulated lymph node cells. To monitor purification, biosynthetically radiolabeled MIF was prepared. Sensitized lymphocytes were stimulated in the presence of [3H]leucine by concanavalin A to produce radiolabeled mediators. MIF was purified approximately 30,000-fold from the culture fluid by using gel filtration, sucrose density gradient electrophoresis, isoelectric focusing, and hydrophobic affinity chromatography. This procedure yielded a single 3H-labeled polypeptide with an apparent Mr of 35,000 that coincides with MIF activity.

References

Feb 1, 1978·The Journal of Experimental Medicine·L H BlockG Ruhenstroth-Bauer
Feb 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·M RubinsteinS Pestka
Aug 29, 1978·Biochemical and Biophysical Research Communications·L W HeckH G Remold
Jul 1, 1974·European Journal of Biochemistry·W M Bonner, R A Laskey
Jul 1, 1966·Proceedings of the National Academy of Sciences of the United States of America·J R David
Mar 1, 1968·Proceedings of the National Academy of Sciences of the United States of America·B Bennett, B R Bloom

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Citations

Jan 1, 1984·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J C Wriston
Aug 1, 1984·The Journal of Experimental Medicine·C F NathanH W Murray
Nov 1, 1982·The Journal of Clinical Investigation·A NakagawaraC F Nathan
Jul 15, 1983·International Journal of Cancer. Journal International Du Cancer·J H RansomC H Evans

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