Bacterial expression of human vitamin D-binding protein (Gc2) in functional form

Protein Expression and Purification
N SwamyR Ray

Abstract

In this report, we report the first expression of human vitamin D-binding protein (hDBP), a serum protein with several functions and a multidomained structure, in Escherichia coli. The recombinant protein (reDBP) was expressed as a fusion partner of glutathione S-transferase in order to facilitate proper folding of the reDBP; E. coli-expressed DBP was found to be fully functional with respect to vitamin D sterol binding, interaction with actin, and cross-reactivity with anti-DBP antibody. Furthermore, both natural DBP and reDBP were affinity-labeled with 25-hydroxyvitamin D3-3-bromo[1-14C]acetate in a similar fashion. Availability of an expression system for hDBP in functional form provides opportunity to develop mutants and truncated DBPs to study multiple ligand-binding properties of this protein in relationship with its structure.

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Citations

Nov 28, 2002·Biological Chemistry·Stefan BuchHans Georg Mannherz
Nov 24, 2007·Biochemical and Biophysical Research Communications·Arjun RayRahul Ray
Mar 10, 2010·Biochimica Et Biophysica Acta·Jianhua ZhangRichard R Kew
Oct 16, 2004·The Journal of Biological Chemistry·Jianhua Zhang, Richard R Kew

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