Abstract
The 79 residue mature surfactant protein B is formed by proteolytic cleavage from a larger precursor. SP-B belongs to the family of saposin-like proteins and has unique functional roles in pulmonary surfactant. The 381-residue human proSP-B fused to an N-terminal poly-His tag was expressed in E. coli, and purified from inclusion bodies by resolubilisation with 2.5% (w/v) SDS followed by metal affinity chromatography after removal of SDS. Recombinant proSP-B solubilised in sodium phosphate buffer exhibits about 35% ±-helical structure and is preferentially proteolytically cleaved between the three tandem saposin-like domains that have been proposed from amino acid sequence comparisons. These results give experimental support to the possibility that proSP-B contains, in addition to SP-B, two further saposin-like domains.
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