Isolation of testosterone-binding globulin from bovine serum by affinity chromatography and its molecular characterization.

Abstract

The testosterone-binding globulin (TeBG) from bovine serum was purified by affinity chromatography and hydroxylapatite chromatography. The affinity column used was prepared by coupling 17 alpha-carboxyethynyl-17-hydroxy-4-androsten-3-one to aminoethyl-Sepharose. The compound was replaceable by 17alpha-carboxyethynyl-17-hydroxy-5alpha-androstan-3-one, but… (More)

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@article{Suzuki1977IsolationOT, title={Isolation of testosterone-binding globulin from bovine serum by affinity chromatography and its molecular characterization.}, author={Yuka Suzuki and Eizi Itagaki and Hiroki Mori and Takaaki Hosoya}, journal={Journal of biochemistry}, year={1977}, volume={81 6}, pages={1721-31} }