Purification of androgen-binding protein from rat testis using high-performance liquid chromatography and physicochemical properties of the iodinated molecule

FEBS Letters
J L GueantJ P Nicolas

Abstract

The androgen-binding protein (ABP) has been purified 87,500-fold from rat testis using 4 steps of HPLC, with a yield of 14%. The molecule was 99% pure with a specific activity estimated to 16,600 pmol/mg protein. The iodinated molecule was eluted in 2 peaks in Sephacryl S300 gel filtration with a molecular mass estimated to be 92,600 +/- 3300 and 50,300 +/- 4000 Da. The column isoelectrofocusing of 125I-ABP demonstrated 3 isoproteins isoelectric at pH 4.7, 4.9 and 5.3 and the sedimentation coefficient was estimated to be 4.7 S in sucrose gradient ultracentrifugation. The 125I-ABP had similar physiochemical properties to the non-labelled ABP of epididymis.

References

Jan 1, 1977·Endocrine Research Communications·N A MustoC W Bardin
Jan 1, 1981·Annual Review of Physiology·C W BardinR Becker

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Citations

Feb 1, 1990·Journal of Steroid Biochemistry·P BarbeyM A Drosdowsky
Jun 1, 1995·The Journal of Steroid Biochemistry and Molecular Biology·A Gerard

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