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Fig. 3 | Molecular Medicine

Fig. 3

From: Purification and Characterization of Macrophage Migration Inhibitory Factor as a Secretory Protein from Rat Epididymis: Evidences for Alternative Release and Transfer to Spermatozoa

Fig. 3

Purification of MIF from rat epididymis. Fractions eluted from the Superdex 75 column were separated using (A) 10% Tricine SDS-PAGE with subsequent silver nitrate staining and (B) parallel Western blots analysis using the antimigration inhibitory factor (MIF) antibody illustrating the MIF purification steps. Lane 1: MIF containing material applied to the Superdex 75 column (25 µg); lane 2: fraction 10 (25 µg); lane 3: fraction 11 (25 µg); lane 4: fraction 12 (25 µg); lane 5: fraction 13 (21 µg); lane 6: fraction 14 (18 µg); lane 7: fraction 15 (5 µg); lane 8: fraction 19 (2 µg); (2–8 fractions eluted from Superdex 75); lane 9: rec MIF (0.5 µg). (C) Alignment of the N-terminal amino acid sequence of the purified 12 kDa protein with the N-terminal sequence of rat MIF (Sakai et al., 1994) revealed a 100% sequence identity.

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Molecular Medicine

ISSN: 1528-3658