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

FEBS Letters

Nicolas, Jean-Pierre¹  Gueant, Jean-Louis¹  Khanfri, Jamal¹  Fremont, Sophie¹  Gerard, Annie¹  Grignon, Georges¹  Gerard, Hubert¹ 

[1] Laboratoire de Biochimie Médicale and Laboratoire d'Histologie-Embryologie, Faculté de Médecine, Université de Nancy I, BP 184, 54505 Vandoeuvre-lès-Nancy Cédex, France

关键词: Androgen-binding protein;    (Testis);    HPLC;    ABP;    androgen-binding protein;    HPLC;    high-performance liquid chromatography;    HP-SEC;    high-performance size-exclusion chromatography;    HPIEC;    high-performance ion-exchange chromatography;    DHT;    5α-dihydrotestosterone;   

DOI  :  10.1016/0014-5793(86)81505-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 physicochemical properties to the non-labelled ABP of epididymis.

【 授权许可】

Unknown