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 Lettjournal_title
FEBS lettersauthors
Gueant JL,Khanfri J,Gerard H,Fremont S,Gerard A,Grignon G,Nicolas JPdoi
10.1016/0014-5793(86)81505-8subject
Has Abstractpub_date
1986-10-27 00:00:00pages
280-6issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(86)81505-8journal_volume
207pub_type
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