SPECIES DEPENDENCY OF THE LIQUID-CHROMATOGRAPHIC PROPERTIES OF SILICA-IMMOBILIZED SERUM ALBUMINS

A series of chemically bonded serum albumins from different animal sou rces (i.e., bovine, human, sheep, and pig) have been prepared via a th ree-step procedure. Subsequently, the differences in the amino acid re sidues forming the binding pockets for L-tryptophan and related analog ues (subdomain mil) were investigated using liquid chromatography. Eve n though there is a high homology among the different species of serum albumins obtained from a number of animal sources, single changes in the relevant sequence were found to significantly alter the proteins' binding selectivity. Van't Hoff plots for both the L- and the D-enanti omers show expected properties. However, changes in the amino acid seq uence are reflected in changes of the specific binding/chromatographic selectivity for differently substituted L-tryptophans.