Similarity of hydrophobic properties of alpha-fetoprotein and albumin.

ABSTRACT

Human alpha-fetoprotein (AFP) and serum albumin (HSA) were studied by hydrophobic interaction chromatography. A close resemblance was observed both in the native state and after various perturbations (pH, salt and alcohol) indicating a significant similarity in their molecular structures. Both proteins displayed similar hydrophobic properties which apparently were different from those of other globular proteins. In agreement with the domain structure proposed by Brown (1976), our results indicated that surface nonpolar side chains of both the native HSA and AFP produced large hydrophobic areas located solely in crevices.