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Protein Science, Vol 5, Issue 10 2074-2079, Copyright © 1996 by Cold Spring Harbor Laboratory Press

ARTICLE

Detection and characterization of an ovine placental lactogen stable intermediate in the urea-induced unfolding process

G. D. CYMES, C. GROSMAN, J. M. DELFINO and C. WOLFENSTEIN-TODEL
Instituto de Quimica y Fisicoquimica Biologicas, Facultad de Farmacia y Bioquimica, UBA, Junin 956, 1113 Buenos Aires, Argentina

The urea-induced equilibrium unfolding of ovine placental lactogen, purified from ovine placenta, was followed by size-exclusion chromatography, far-UV CD, and intrinsic tryptophan fluorescence. The data obtained by each of these methods showed a poor fit to a two-state model involving only a native and an unfolded form. A satisfactory fit required, instead, a model that involved a stable, partially folded form in addition to the native and unfolded ones. The results obtained from the best-fitting theoretical curves for the three-state model indicated that this intermediate state, which is the predominant species in solution at 3.6 M of urea activity, is compact, largely {alpha}-helical, and changes considerably the native-like tertiary packing around its tryptophan residues. These findings suggest that this stable intermediate exhibits properties similar to those that characterize the molten globule state.
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