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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Heterologous overexpression of human NEFA and studies on the two EF-hand calcium-binding sites.

Human NEFA is an EF-hand, leucine zipper protein containing a signal sequence. To confirm the calcium binding capacity of NEFA, recombinant NEFA analogous to the mature protein and mutants with deletions in the EF-hand domain were expressed in Pichia pastoris and secreted into the culture medium at high yield. The calcium binding activity of each purified protein was measured by a modified equilibrium dialysis using the fluorescent Ca2+ indicator FURA-2 and atomic absorption spectroscopy. A stoichiometry of 2 mol Ca2+/mol NEFA was determined. The Ca2+ binding constants were resolved by intrinsic fluorescence spectroscopy. Fluorescence titration exhibited two classes of Ca2+ binding sites with Kd values of 0.08 microM and 0.2 microM. Circular dichroism (CD) spectroscopy showed an increase from 30 to 43% in the amount of alpha-helix in NEFA after addition of calcium ions. Limited proteolytic digestion indicated a Ca2+ dependent conformational change accompanied by an altered accessibility to the enzyme.[1]


  1. Heterologous overexpression of human NEFA and studies on the two EF-hand calcium-binding sites. Kroll, K.A., Otte, S., Hirschfeld, G., Barnikol-Watanabe, S., Götz, H., Sternbach, H., Kratzin, H.D., Barnikol, H.U., Hilschmann, N. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
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