| First Author | Galat A | Year | 1994 |
| Journal | Eur J Biochem | Volume | 224 |
| Issue | 2 | Pages | 417-21 |
| PubMed ID | 7925355 | Mgi Jnum | J:20695 |
| Mgi Id | MGI:68770 | Doi | 10.1111/j.1432-1033.1994.00417.x |
| Citation | Galat A, et al. (1994) A diversified family of 12-kDa proteins with a high amino acid sequence similarity to macrophage migration-inhibitory factor (MIF). Eur J Biochem 224(2):417-21 |
| abstractText | Two isoforms of a bovine-brain-derived 12-kDa protein (designated p12a and p12b) whose N-termini have a high amino acid sequence similarity with the glycosylation-inhibiting factor (GIF) and macrophage migration-inhibitory factor (MIF) were purified to homogeneity. The complete amino acid sequence of bovine p12a (pI 9.5) was determined by Edman degradation of the intact molecule and overlapping fragments generated by proteolytic cleavage. The p12a isoform has nine and ten conservative substitutions versus human GIF (hGIF) and human MIF (hMIF), respectively. Molecular filtration revealed that both isoforms of p12 exist as monomers in aqueous solution. Circular dichroism spectra indicate that both isoforms of p12 consist of 39 +/- 3% alpha helix, 23 +/- 3% beta structure and 15 +/- 3% beta turns. Although the N-terminal parts of p12a and p12b have weak amino acid sequence similarity with that of glutathione S-transferase (GST) neither isoform of p12 was bound to a GST-affinity gel nor had GST activity. Despite a high amino acid sequence similarity with human MIF neither of the p12 isoforms inhibited migration of the mouse monocyte-macrophage cells P338D1. |
