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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Gueant JL,Khanfri J,Gerard H,Fremont S,Gerard A,Grignon G,Nicolas JP

doi

10.1016/0014-5793(86)81505-8

subject

Has Abstract

pub_date

1986-10-27 00:00:00

pages

280-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)81505-8

journal_volume

207

pub_type

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