Species dependency of the liquid chromatographic properties of silica-immobilized serum albumins.
A series of chemically bonded serum albumins from different animal sources (i.e., bovine, human, sheep, and pig) have been prepared via a three-step procedure. Subsequently, the differences in the amino acid residues forming the binding pockets for L-tryptophan and related analogues (subdomain IIIA) were investigated using liquid chromatography. Even 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-enantiomers show expected properties. However, changes in the amino acid sequence are reflected in changes of the specific binding/chromatographic selectivity for differently substituted L-tryptophans.
Tittelbach
V
V
Department of Chemistry, Kent State University, Ohio 44242.
Gilpin
R K
RK
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002853:Chromatography, Liquid / Q000379:methods; D002942:Circular Dichroism; D006801:Humans; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D012756:Sheep; D013045:Species Specificity; D013237:Stereoisomerism; D013552:Swine; D014364:Tryptophan / Q000302:isolation & purification / Q000378:metabolism
D012709:Serum Albumin; D014364:Tryptophan