Author(s): Bashor MM, Hewett J, Lackey A, Driskell WJ, Neese JW
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Abstract A method is presented by which prealbumin (thyroxine-binding prealbumin; tryptophan-rich prealbumin) may be purified to homogeneity from human serum. The method involves precipitation of contaminating proteins with dilute aqueous phenol, ion-exchange chromatography on DEAE-Sephacel, and gel permeation chromatography on Sephadex G-100. The yield is 25-30\%, and the prealbumin is homogeneous by polyacrylamide gel electrophoresis at pH 8.9 and pH 3.6.
This article was published in Prep Biochem
and referenced in Biochemistry & Pharmacology: Open Access