1. Prealbumin, a thyroxine-binding protein, is known to bind also to retinol-binding protein and is suspected on X-ray-crystallographic evidence of having a quaternary structure. 2. Experiments described in this paper suggest that the molecule is a tetramer of mol.wt. about 56000, which is disaggregated with some difficulty into subunits of mol.wt. about 14000. 3. The number and staining properties of the tryptic peptides indicate that the subunits are identical or closely similar. This conclusion is reinforced by comparing the sum of the amino acid compositions of the tryptic peptides with the amino acid composition of the whole protein. All minor peptides that were isolated could be shown to be derived from major peptides. 4. No evidence has been found, either from electrophoretic experiments or from amino acid sequence determination, for any dissimilarity between the subunits.

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Author notes

*On leave of absence (1968–72) from Departamento de Quimica, Universidad de Chile-Casilla 130-V, Valparaiso, Chile.