Macrophage migration inhibitory factor (MIF) produced by a human T cell hybridoma clone.

Abstract:

:A human T cell hybridoma clone, F5, producing high levels of macrophage migration inhibitory factor (MIF) was established by the emetine-actinomycin D selection method. This clone produced two species of MIF which were separated on a Phenyl Sepharose column. We purified MIF-2 (the more hydrophobic species of the two) to homogeneity from the conditioned medium of stimulated F5 cells by a series of steps that included hydrophobic chromatography, ion-exchange chromatography. Ricinus communis lectin affinity chromatography, and high-performance liquid chromatography on anion exchange and reverse-phase columns. Purified MIF was digested with endoproteinase Lys-C and Asp-N. The amino acid sequences of the generated peptides were determined. No sequence similarity with any other protein was found. The molecular weight of MIF-2 was estimated to be 45 kDa from sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of immunoprecipitates with anti-peptide antibodies. These results show that F5MIF-2 is a novel cytokine.

journal_name

Microbiol Immunol

authors

Hirose S,Ooki S,Higuchi M,Osawa T

doi

10.1111/j.1348-0421.1991.tb01552.x

subject

Has Abstract

pub_date

1991-01-01 00:00:00

pages

235-45

issue

3

eissn

0385-5600

issn

1348-0421

journal_volume

35

pub_type

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