Evidence for a testosterone binding macromolecule in human placental cytosol
Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein conce...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1979 |
|---|
| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Journal of Steroid Biochemistry - Amsterdam : Elsevier, 11(1979), 3, Seite 1247-1252 |
| Übergeordnetes Werk: |
volume:11 ; year:1979 ; number:3 ; pages:1247-1252 |
| Links: |
|---|
| Katalog-ID: |
NLEJ186351909 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ186351909 | ||
| 003 | DE-627 | ||
| 005 | 20210707043153.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 070506s1979 xx |||||o 00| ||eng c | ||
| 035 | |a (DE-627)NLEJ186351909 | ||
| 035 | |a (DE-599)GBVNLZ186351909 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 245 | 1 | 0 | |a Evidence for a testosterone binding macromolecule in human placental cytosol |
| 264 | 1 | |c 1979 | |
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. | ||
| 533 | |f Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 | ||
| 700 | 1 | |a Barile, G. |4 oth | |
| 700 | 1 | |a Giani, S. |4 oth | |
| 700 | 1 | |a Montemurro, A. |4 oth | |
| 700 | 1 | |a Mango, D. |4 oth | |
| 700 | 1 | |a Scirpa, P. |4 oth | |
| 773 | 0 | 8 | |i in |t Journal of Steroid Biochemistry |d Amsterdam : Elsevier |g 11(1979), 3, Seite 1247-1252 |w (DE-627)NLEJ18527725X |w (DE-600)2198730-0 |x 0022-4731 |7 nnns |
| 773 | 1 | 8 | |g volume:11 |g year:1979 |g number:3 |g pages:1247-1252 |
| 856 | 4 | 0 | |u http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4 |
| 912 | |a GBV_USEFLAG_H | ||
| 912 | |a ZDB-1-SDJ | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 11 |j 1979 |e 3 |h 1247-1252 | ||
| matchkey_str |
article:00224731:1979----::vdneoaetseoeidnmcooeuenu |
|---|---|
| hierarchy_sort_str |
1979 |
| publishDate |
1979 |
| allfields |
(DE-627)NLEJ186351909 (DE-599)GBVNLZ186351909 DE-627 ger DE-627 rakwb eng Evidence for a testosterone binding macromolecule in human placental cytosol 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Barile, G. oth Giani, S. oth Montemurro, A. oth Mango, D. oth Scirpa, P. oth in Journal of Steroid Biochemistry Amsterdam : Elsevier 11(1979), 3, Seite 1247-1252 (DE-627)NLEJ18527725X (DE-600)2198730-0 0022-4731 nnns volume:11 year:1979 number:3 pages:1247-1252 http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 11 1979 3 1247-1252 |
| spelling |
(DE-627)NLEJ186351909 (DE-599)GBVNLZ186351909 DE-627 ger DE-627 rakwb eng Evidence for a testosterone binding macromolecule in human placental cytosol 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Barile, G. oth Giani, S. oth Montemurro, A. oth Mango, D. oth Scirpa, P. oth in Journal of Steroid Biochemistry Amsterdam : Elsevier 11(1979), 3, Seite 1247-1252 (DE-627)NLEJ18527725X (DE-600)2198730-0 0022-4731 nnns volume:11 year:1979 number:3 pages:1247-1252 http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 11 1979 3 1247-1252 |
| allfields_unstemmed |
(DE-627)NLEJ186351909 (DE-599)GBVNLZ186351909 DE-627 ger DE-627 rakwb eng Evidence for a testosterone binding macromolecule in human placental cytosol 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Barile, G. oth Giani, S. oth Montemurro, A. oth Mango, D. oth Scirpa, P. oth in Journal of Steroid Biochemistry Amsterdam : Elsevier 11(1979), 3, Seite 1247-1252 (DE-627)NLEJ18527725X (DE-600)2198730-0 0022-4731 nnns volume:11 year:1979 number:3 pages:1247-1252 http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 11 1979 3 1247-1252 |
| allfieldsGer |
(DE-627)NLEJ186351909 (DE-599)GBVNLZ186351909 DE-627 ger DE-627 rakwb eng Evidence for a testosterone binding macromolecule in human placental cytosol 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Barile, G. oth Giani, S. oth Montemurro, A. oth Mango, D. oth Scirpa, P. oth in Journal of Steroid Biochemistry Amsterdam : Elsevier 11(1979), 3, Seite 1247-1252 (DE-627)NLEJ18527725X (DE-600)2198730-0 0022-4731 nnns volume:11 year:1979 number:3 pages:1247-1252 http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 11 1979 3 1247-1252 |
| allfieldsSound |
(DE-627)NLEJ186351909 (DE-599)GBVNLZ186351909 DE-627 ger DE-627 rakwb eng Evidence for a testosterone binding macromolecule in human placental cytosol 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Barile, G. oth Giani, S. oth Montemurro, A. oth Mango, D. oth Scirpa, P. oth in Journal of Steroid Biochemistry Amsterdam : Elsevier 11(1979), 3, Seite 1247-1252 (DE-627)NLEJ18527725X (DE-600)2198730-0 0022-4731 nnns volume:11 year:1979 number:3 pages:1247-1252 http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 11 1979 3 1247-1252 |
| language |
English |
| source |
in Journal of Steroid Biochemistry 11(1979), 3, Seite 1247-1252 volume:11 year:1979 number:3 pages:1247-1252 |
| sourceStr |
in Journal of Steroid Biochemistry 11(1979), 3, Seite 1247-1252 volume:11 year:1979 number:3 pages:1247-1252 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Journal of Steroid Biochemistry |
| authorswithroles_txt_mv |
Barile, G. @@oth@@ Giani, S. @@oth@@ Montemurro, A. @@oth@@ Mango, D. @@oth@@ Scirpa, P. @@oth@@ |
| publishDateDaySort_date |
1979-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ18527725X |
| id |
NLEJ186351909 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ186351909</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707043153.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1979 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186351909</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186351909</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Evidence for a testosterone binding macromolecule in human placental cytosol</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1979</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Barile, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Giani, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Montemurro, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mango, D.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Scirpa, P.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of Steroid Biochemistry</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">11(1979), 3, Seite 1247-1252</subfield><subfield code="w">(DE-627)NLEJ18527725X</subfield><subfield code="w">(DE-600)2198730-0</subfield><subfield code="x">0022-4731</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:11</subfield><subfield code="g">year:1979</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:1247-1252</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">11</subfield><subfield code="j">1979</subfield><subfield code="e">3</subfield><subfield code="h">1247-1252</subfield></datafield></record></collection>
|
| series2 |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ18527725X |
| format |
electronic Article |
| delete_txt_mv |
keep |
| collection |
NL |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
0022-4731 |
| topic_title |
Evidence for a testosterone binding macromolecule in human placental cytosol |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
g b gb s g sg a m am d m dm p s ps |
| hierarchy_parent_title |
Journal of Steroid Biochemistry |
| hierarchy_parent_id |
NLEJ18527725X |
| hierarchy_top_title |
Journal of Steroid Biochemistry |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ18527725X (DE-600)2198730-0 |
| title |
Evidence for a testosterone binding macromolecule in human placental cytosol |
| spellingShingle |
Evidence for a testosterone binding macromolecule in human placental cytosol |
| ctrlnum |
(DE-627)NLEJ186351909 (DE-599)GBVNLZ186351909 |
| title_full |
Evidence for a testosterone binding macromolecule in human placental cytosol |
| journal |
Journal of Steroid Biochemistry |
| journalStr |
Journal of Steroid Biochemistry |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1979 |
| contenttype_str_mv |
zzz |
| container_start_page |
1247 |
| container_volume |
11 |
| format_se |
Elektronische Aufsätze |
| title_sort |
evidence for a testosterone binding macromolecule in human placental cytosol |
| title_auth |
Evidence for a testosterone binding macromolecule in human placental cytosol |
| abstract |
Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. |
| abstractGer |
Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. |
| abstract_unstemmed |
Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested. |
| collection_details |
GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE |
| container_issue |
3 |
| title_short |
Evidence for a testosterone binding macromolecule in human placental cytosol |
| url |
http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4 |
| remote_bool |
true |
| author2 |
Barile, G. Giani, S. Montemurro, A. Mango, D. Scirpa, P. |
| author2Str |
Barile, G. Giani, S. Montemurro, A. Mango, D. Scirpa, P. |
| ppnlink |
NLEJ18527725X |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth oth oth |
| up_date |
2024-07-06T06:41:15.364Z |
| _version_ |
1803810845873930240 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ186351909</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707043153.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1979 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186351909</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186351909</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Evidence for a testosterone binding macromolecule in human placental cytosol</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1979</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Specific binding of [^3H]-testosterone was found in the human placental cytosol. At a [^3H]-testosterone concentration of 3 x 10^-^8M, the binding was maximal after 1h and remained at that level for at least 24 h. [^3H]-testosterone binding was linearly related to the amount of cytosol protein concentration up to 4.0 mg/ml. Kinetic analysis revealed the presence of specific binding sites with a K"D of 11.7 x 10^-^9 M and a concentration of binding sites of 306 fmol/mg protein. The [^3H]-testosterone macromolecule complex exhibited a sedimentation coefficient of 4.6 S under low and high salt conditions. The 4.6 S radioactivity peak disappeared after treatment at 45^oC for 1h and was inhibited or suppressed by a 10 or 1000 fold excess of cold testosterone. In competitive binding studies cold testosterone, 5α-dihydrotestosterone, androstenedione and dehydroepiandrosterone were the most active competitors. The fact that estradiol also competes for [^3H]-testosterone binding, but binds to this cytoplasmic component only to a small extent, indicates that the macromolecule studied is not SHBG. The possible role of this macro-molecule as an androgen receptor in the human placenta is suggested.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Barile, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Giani, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Montemurro, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mango, D.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Scirpa, P.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of Steroid Biochemistry</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">11(1979), 3, Seite 1247-1252</subfield><subfield code="w">(DE-627)NLEJ18527725X</subfield><subfield code="w">(DE-600)2198730-0</subfield><subfield code="x">0022-4731</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:11</subfield><subfield code="g">year:1979</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:1247-1252</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0022-4731(79)90192-4</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">11</subfield><subfield code="j">1979</subfield><subfield code="e">3</subfield><subfield code="h">1247-1252</subfield></datafield></record></collection>
|
| score |
7.399457 |