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Testicular androgen binding protein (ABP) was purified from the epididymis of 1500 adult rabbits by the sequential use of ammonium sulphate precipitation, ion exchange chromatography on DEAE cellulose, gel filtration on Sephadex G-200, hydroxyl-apatite chromatography and preparative polyacrylamide gel electrophoresis. This procedure yielded a 1000-fold increase in specific activity compared to that of the 1500,000 x g supernatant, and the recovery of active ABP was about 3-5%. ABP is acid glycoprotein with a molecular weight of 65-68,000 daltons. Antisera to rabbit ABP raised in quinea pigs inhibit 3H-DHT binding to ABP as measured by SS-PAGE. When diluted rabbit serum containing TeBG is treated with the same dilutions of these antisera, identical binding inhibition curves are found. Thus, ABP and TeBG in rabbits appear to possess identical immunological determinants.
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July 1975,
Molecular and cellular endocrinology,
S C Weddington, and
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May 1975,
Molecular and cellular endocrinology,
S C Weddington, and
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July 1974,
Steroids,
S C Weddington, and
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V Hansson
October 1977,
Molecular and cellular endocrinology,
S C Weddington, and
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August 1975,
Endocrinology,
S C Weddington, and
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May 1982,
Biochemistry,
S C Weddington, and
P Brandtzaeg, and
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V Hansson
January 1975,
Current topics in molecular endocrinology,
S C Weddington, and
P Brandtzaeg, and
K Sletten, and
T Christensen, and
V Hansson
January 1975,
Current topics in molecular endocrinology,
S C Weddington, and
P Brandtzaeg, and
K Sletten, and
T Christensen, and
V Hansson
January 1974,
Current topics in molecular endocrinology,
S C Weddington, and
P Brandtzaeg, and
K Sletten, and
T Christensen, and
V Hansson
April 1981,
International journal of andrology,
