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Partition of purified human thyroxine-binding globulin in aqueous two-phase systems in response to reactive dyes

✍ Scribed by G. Birkenmeier; U. Ehrlich; G. Kopperschläger; G. Appelt

Book ID: 104143839
Publisher: Elsevier Science
Year: 1986
Tongue: English
Weight: 676 KB
Volume: 360
Category: Article
ISSN: 1873-3778
DOI: 10.1016/s0021-9673(00)91662-5

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✦ Synopsis

Thyroxine-binding globulin was isolated from pooled human serum by a twostep method involving affinity chromatography on thyroxine-Sepharose and preparative disc-electrophoresis. The final product was found to be homogeneous by polyacrylamide gel electrophoresis and has a molecular weight of 59 000. Isoelectric focusing resolved the protein into seven bands with isoelectric points ranging from 3.9 to 4.3.

The isolated protein showed affinity to a number of different dyes as recognized by affinity phase partitioning. The interaction of the protein with the dye Cibacron Blue F3G-A was found to be strongly competitive with the natural ligand thyroxine.

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