Identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa
Androgen-dependent epididymal proteins were investigated in the hamster. The stimulation of labelled amino acid incorporation, as well as the colour intensity of bands stained with Coomassie Blue after electrophoresis of the epididymal cytosol from castrated animals with and without androgen replace...
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1982
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224251_v64_n1_p1_GonzalezEcheverria http://hdl.handle.net/20.500.12110/paper_00224251_v64_n1_p1_GonzalezEcheverria |
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paper:paper_00224251_v64_n1_p1_GonzalezEcheverria2023-06-08T14:50:51Z Identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa androgen glycoprotein radioisotope amino acid c 14 amino acid h 3 animal experiment endocrine system epididymis male genital system spermatozoon Amino Acids Animal Castration Electrophoresis, Polyacrylamide Gel Epididymis Glycoproteins Hamsters Male Mesocricetus Molecular Weight Spermatozoa Support, Non-U.S. Gov't Testosterone Androgen-dependent epididymal proteins were investigated in the hamster. The stimulation of labelled amino acid incorporation, as well as the colour intensity of bands stained with Coomassie Blue after electrophoresis of the epididymal cytosol from castrated animals with and without androgen replacement, were used as semi-quantitative criteria for evaluation. These techniques allowed the identification of 6 androgen-sensitive bands (EP) with the following relative electrophoretic mobilities with respect to albumin: EP1 = 0.8; EP2 = 1.11; EP3 = 1.21; EP4 = 1.31; EP5 = 1.52; EP6 = 1.63. The proteins EP1, EP3 and EP4 were also found in fluid from the cauda epididymidis. Extraction of spermatozoa from the distal corpus and cauda epididymidis with 0.25 and 0.5 M-NaCl yielded appreciable amounts of EP2 and EP3 but these bands were not detected in extracts of spermatozoa from proximal segments. The approximate molecular weights were 61 400 for EP1, 42 500 for EP2, 23 800 for EP3, 20 400 for EP4, 26 100 for EP5 and 41 000 for EP6. All bands stained as glycoproteins with periodic acid-Schiff reagent. 1982 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224251_v64_n1_p1_GonzalezEcheverria http://hdl.handle.net/20.500.12110/paper_00224251_v64_n1_p1_GonzalezEcheverria |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
androgen glycoprotein radioisotope amino acid c 14 amino acid h 3 animal experiment endocrine system epididymis male genital system spermatozoon Amino Acids Animal Castration Electrophoresis, Polyacrylamide Gel Epididymis Glycoproteins Hamsters Male Mesocricetus Molecular Weight Spermatozoa Support, Non-U.S. Gov't Testosterone |
| spellingShingle |
androgen glycoprotein radioisotope amino acid c 14 amino acid h 3 animal experiment endocrine system epididymis male genital system spermatozoon Amino Acids Animal Castration Electrophoresis, Polyacrylamide Gel Epididymis Glycoproteins Hamsters Male Mesocricetus Molecular Weight Spermatozoa Support, Non-U.S. Gov't Testosterone Identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa |
| topic_facet |
androgen glycoprotein radioisotope amino acid c 14 amino acid h 3 animal experiment endocrine system epididymis male genital system spermatozoon Amino Acids Animal Castration Electrophoresis, Polyacrylamide Gel Epididymis Glycoproteins Hamsters Male Mesocricetus Molecular Weight Spermatozoa Support, Non-U.S. Gov't Testosterone |
| description |
Androgen-dependent epididymal proteins were investigated in the hamster. The stimulation of labelled amino acid incorporation, as well as the colour intensity of bands stained with Coomassie Blue after electrophoresis of the epididymal cytosol from castrated animals with and without androgen replacement, were used as semi-quantitative criteria for evaluation. These techniques allowed the identification of 6 androgen-sensitive bands (EP) with the following relative electrophoretic mobilities with respect to albumin: EP1 = 0.8; EP2 = 1.11; EP3 = 1.21; EP4 = 1.31; EP5 = 1.52; EP6 = 1.63. The proteins EP1, EP3 and EP4 were also found in fluid from the cauda epididymidis. Extraction of spermatozoa from the distal corpus and cauda epididymidis with 0.25 and 0.5 M-NaCl yielded appreciable amounts of EP2 and EP3 but these bands were not detected in extracts of spermatozoa from proximal segments. The approximate molecular weights were 61 400 for EP1, 42 500 for EP2, 23 800 for EP3, 20 400 for EP4, 26 100 for EP5 and 41 000 for EP6. All bands stained as glycoproteins with periodic acid-Schiff reagent. |
| title |
Identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa |
| title_short |
Identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa |
| title_full |
Identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa |
| title_fullStr |
Identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa |
| title_full_unstemmed |
Identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa |
| title_sort |
identification of androgen-dependent glycoproteins in the hamster epididymis and their association with spermatozoa |
| publishDate |
1982 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224251_v64_n1_p1_GonzalezEcheverria http://hdl.handle.net/20.500.12110/paper_00224251_v64_n1_p1_GonzalezEcheverria |
| _version_ |
1768544443346976768 |