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High Level Expression and Dimer Characterization of the S100 EF-hand Proteins, Migration Inhibitory Factor-related Proteins 8 and 14

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Hunter, Michael J., Chazin, Walter J.·1998·Journal of Biological Chemistry

Abstract

The phenotypical and functional heterogeneity of different macrophage subpopulations are defined by discrete changes in the expression of two S100 calcium-binding proteins, migration inhibitory factor-related proteins (MRPs) 8 and 14. To further our understanding of MRP8 and MRP14 in the developmental stages of inflammatory responses, overexpression of the MRPs was obtained through a combination of a T7-based expression vector and the Escherichia coli BL21 (DE3) cell line. An efficient, two-step chromatographic protocol was then developed for rapid, facile purification. Extensive biophysical characterization and chemical cross-linking experiments show that MRP8 and MRP14 form oligomers with a strong preference to associate as a heterodimer. Heteronuclear NMR experiments indicate that a specific well packed dimer is formed only in equimolar mixtures of the two proteins. Our results suggest that there is a unique complementarity in the interface of the MRP8/MRP14 complex that cannot be fully reproduced in the MRP8 and MRP14 homodimers.

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Metadata

Authors
Hunter, M. J., & Chazin, W. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-05
Volume
273
Issue
20
Pages
12427-12435
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1995166771
Cited by
216
References
0
FWCI
2.36
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: High Level Expression and Dimer Characterization of the S100 EF-hand Proteins, Migration Inhibitory Factor-related Proteins 8 and 14. https://app.cochat.ai/papers/10.1074/jbc.273.20.12427
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Hunter, M. J., & Chazin, W. J. (1998). High Level Expression and Dimer Characterization of the S100 EF-hand Proteins, Migration Inhibitory Factor-related Proteins 8 and 14. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.20.12427

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