Biomaterial Database

Androgen-binding activity in the human testis and epididymis. 1977

L I Lipshultz, and Y H Tsai, and B M Sanborn, and E Steinberger

The quantitation of androgen-binding activity in human testes, epididymides, and serum is reported and compared with that of similar tissue in the rat. By using steady-state polyacrylamide gel electrophoresis and a tritiated 0.5 nM testosterone label, values for specific binding activity, reported as picomoles per milligram of protein, were found to be 0.21 +/- 0.01 in normal human, epididymides, 0.03 in testes, and 0.44 +/- 0.07 in human serum. Tissues from men receiving exogenous estrogen were also similarly analyzed and found to possess significantly higher androgen-binding activity: 4.10 +/- 0.48 pmoles/mg of protein (epididymides), 4.01 (testes), and 5.63 +/- 1.15 (serum). Since man possesses a sex steroid-binding globulin, attempts were made to differentiate Ion-exchange chromatography, steroid specificity, and dissociation half-time determinations were suggestive but did not conclusively demonstrate the existence of two distinctly different androgen transport macromolecules in man.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D002852	Chromatography, Ion Exchange	Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.	Chromatography, Ion-Exchange,Ion-Exchange Chromatography,Chromatographies, Ion Exchange,Chromatographies, Ion-Exchange,Ion Exchange Chromatographies,Ion Exchange Chromatography,Ion-Exchange Chromatographies
D003600	Cytosol	Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.	Cytosols
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D004822	Epididymis	The convoluted cordlike structure attached to the posterior of the TESTIS. Epididymis consists of the head (caput), the body (corpus), and the tail (cauda). A network of ducts leaving the testis joins into a common epididymal tubule proper which provides the transport, storage, and maturation of SPERMATOZOA.
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000728	Androgens	Compounds that interact with ANDROGEN RECEPTORS in target tissues to bring about the effects similar to those of TESTOSTERONE. Depending on the target tissues, androgenic effects can be on SEX DIFFERENTIATION; male reproductive organs, SPERMATOGENESIS; secondary male SEX CHARACTERISTICS; LIBIDO; development of muscle mass, strength, and power.	Androgen,Androgen Receptor Agonist,Androgen Effect,Androgen Effects,Androgen Receptor Agonists,Androgenic Agents,Androgenic Compounds,Agents, Androgenic,Agonist, Androgen Receptor,Agonists, Androgen Receptor,Compounds, Androgenic,Effect, Androgen,Effects, Androgen,Receptor Agonist, Androgen,Receptor Agonists, Androgen
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D012738	Sex Hormone-Binding Globulin	A glycoprotein migrating as a beta-globulin. Its molecular weight, 52,000 or 95,000-115,000, indicates that it exists as a dimer. The protein binds testosterone, dihydrotestosterone, and estradiol in the plasma. Sex hormone-binding protein has the same amino acid sequence as ANDROGEN-BINDING PROTEIN. They differ by their sites of synthesis and post-translational oligosaccharide modifications.	Sex Steroid-Binding Protein,Testosterone-Estradiol Binding Globulin,Binding Globulin, Testosterone-Estradiol,Globulin, Sex Hormone-Binding,Globulin, Testosterone-Estradiol Binding,Hormone-Binding Globulin, Sex,Sex Hormone Binding Globulin,Sex Steroid Binding Protein,Steroid-Binding Protein, Sex,Testosterone Estradiol Binding Globulin