Solubilization of pituitary receptors for thyrotropin-releasing hormone
Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone s...
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1978 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/General Subjects - Amsterdam : Elsevier, 541(1978), 3, Seite 347-359 |
| Übergeordnetes Werk: |
volume:541 ; year:1978 ; number:3 ; pages:347-359 |
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| 520 | |a Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. | ||
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(DE-627)NLEJ187048215 (DE-599)GBVNLZ187048215 DE-627 ger DE-627 rakwb eng Solubilization of pituitary receptors for thyrotropin-releasing hormone 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hinkle, P.M. oth Lewis, D.G. oth in Biochimica et Biophysica Acta (BBA)/General Subjects Amsterdam : Elsevier 541(1978), 3, Seite 347-359 (DE-627)NLEJ177008172 (DE-600)2209617-6 0304-4165 nnns volume:541 year:1978 number:3 pages:347-359 http://linkinghub.elsevier.com/retrieve/pii/0304-4165(78)90194-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 541 1978 3 347-359 |
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(DE-627)NLEJ187048215 (DE-599)GBVNLZ187048215 DE-627 ger DE-627 rakwb eng Solubilization of pituitary receptors for thyrotropin-releasing hormone 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hinkle, P.M. oth Lewis, D.G. oth in Biochimica et Biophysica Acta (BBA)/General Subjects Amsterdam : Elsevier 541(1978), 3, Seite 347-359 (DE-627)NLEJ177008172 (DE-600)2209617-6 0304-4165 nnns volume:541 year:1978 number:3 pages:347-359 http://linkinghub.elsevier.com/retrieve/pii/0304-4165(78)90194-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 541 1978 3 347-359 |
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(DE-627)NLEJ187048215 (DE-599)GBVNLZ187048215 DE-627 ger DE-627 rakwb eng Solubilization of pituitary receptors for thyrotropin-releasing hormone 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hinkle, P.M. oth Lewis, D.G. oth in Biochimica et Biophysica Acta (BBA)/General Subjects Amsterdam : Elsevier 541(1978), 3, Seite 347-359 (DE-627)NLEJ177008172 (DE-600)2209617-6 0304-4165 nnns volume:541 year:1978 number:3 pages:347-359 http://linkinghub.elsevier.com/retrieve/pii/0304-4165(78)90194-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 541 1978 3 347-359 |
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(DE-627)NLEJ187048215 (DE-599)GBVNLZ187048215 DE-627 ger DE-627 rakwb eng Solubilization of pituitary receptors for thyrotropin-releasing hormone 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hinkle, P.M. oth Lewis, D.G. oth in Biochimica et Biophysica Acta (BBA)/General Subjects Amsterdam : Elsevier 541(1978), 3, Seite 347-359 (DE-627)NLEJ177008172 (DE-600)2209617-6 0304-4165 nnns volume:541 year:1978 number:3 pages:347-359 http://linkinghub.elsevier.com/retrieve/pii/0304-4165(78)90194-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 541 1978 3 347-359 |
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(DE-627)NLEJ187048215 (DE-599)GBVNLZ187048215 DE-627 ger DE-627 rakwb eng Solubilization of pituitary receptors for thyrotropin-releasing hormone 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hinkle, P.M. oth Lewis, D.G. oth in Biochimica et Biophysica Acta (BBA)/General Subjects Amsterdam : Elsevier 541(1978), 3, Seite 347-359 (DE-627)NLEJ177008172 (DE-600)2209617-6 0304-4165 nnns volume:541 year:1978 number:3 pages:347-359 http://linkinghub.elsevier.com/retrieve/pii/0304-4165(78)90194-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 541 1978 3 347-359 |
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solubilization of pituitary receptors for thyrotropin-releasing hormone |
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Solubilization of pituitary receptors for thyrotropin-releasing hormone |
| abstract |
Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. |
| abstractGer |
Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. |
| abstract_unstemmed |
Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ187048215</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707064454.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1978 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ187048215</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ187048215</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">Solubilization of pituitary receptors for thyrotropin-releasing hormone</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1978</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">Receptors for thyrotropin-releasing hormone were solubilized by Triton X-100. Membrane fractions from GH"3 pituitary tumor cells were incubated with thyrotropin-releasing hormone in order to saturate specific receptor sites before the addition of detergent. The amount of protein-bound hormone solubilized by Triton X-100 was proportional to the fractional saturation of specific membrane receptors. Increasing detergent: protein ratios from 0.5 to 20 led to a progressive loss of hormone . receptor complex from membrane fractions with a concomitant increase in soluble protein-bound hormone. The soluble hormone . receptor complex was not retained by 0.22 μm filters and remained soluble after ultracentrifugation. Following incubation with high (2.5-10%) concentration of Triton X-100 and other non-ionic detergents, or following repeated detergent extraction, at least 18% of specifically bound thyrotropin-releasing hormone remained associated with particulate material. Unlike the hormone receptor complex, the free hormone receptor was inactivated by Triton X-100. A 50% loss of binding activity was obtained with 0.01% Triton X-100, corresponding to a detergent: protein ratio of 0.033.The hormone . receptor complex was included in Sepharose 6B and exhibited an apparent Stokes radius of 46 Å in buffers containing Triton X-100. The complex aggregated in detergent-free buffers. Soluble hormone receptors were separated from excess detergent and thyrotropin-releasing hormone by chromatography on DEAE-cellulose. Thyrotropin-releasing hormone dissociated from soluble receptors with a half-time of 120 min at 0^oc, while the membrane hormone . receptor complex was stable for up to 5 h at 0^oC.</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">Hinkle, P.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lewis, D.G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/General Subjects</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">541(1978), 3, Seite 347-359</subfield><subfield code="w">(DE-627)NLEJ177008172</subfield><subfield code="w">(DE-600)2209617-6</subfield><subfield code="x">0304-4165</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:541</subfield><subfield code="g">year:1978</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:347-359</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0304-4165(78)90194-0</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">541</subfield><subfield code="j">1978</subfield><subfield code="e">3</subfield><subfield code="h">347-359</subfield></datafield></record></collection>
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| score |
7.401764 |