Purification of androgen-binding protein from rat testis using high-performance liquid chromatography and physicochemical properties of the iodinated molecule
| Autor: | Hubert Gerard, Jean-Pierre Nicolas, Sophie Fremont, Georges Grignon, Jamal Khanfri, Annie Gerard, Jean-Louis Guéant |
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| Rok vydání: | 1986 |
| Předmět: |
Male
Chemical Phenomena Androgen-binding protein genetic structures Size-exclusion chromatography Biophysics Biochemistry High-performance liquid chromatography Iodine Radioisotopes Structural Biology Testis Centrifugation Density Gradient Genetics Animals Molecular Biology Chromatography High Pressure Liquid (Testis) Chromatography Molecular mass Chemistry Physical Chemistry Elution Binding protein Cell Biology Rats Molecular Weight Sedimentation coefficient Isoelectric point Chromatography Gel Ultracentrifuge Isoelectric Focusing HPLC |
| Zdroj: | FEBS Letters. 207:280-286 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(86)81505-8 |
| Popis: | 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 125 I-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 125 I-ABP had similar physicochemical properties to the non-labelled ABP of epididymis. |
| Databáze: | OpenAIRE |
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