Lack of adenylate and guanylate cyclases responsiveness to hormones in a spontaneous murine thyroid tumor
Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to...
Ausführliche Beschreibung
Gespeichert in:
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E-Artikel |
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Englisch |
| Erschienen: |
1980 |
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Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 95(1980), 1, Seite 357-366 |
| Übergeordnetes Werk: |
volume:95 ; year:1980 ; number:1 ; pages:357-366 |
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| 520 | |a Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. | ||
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(DE-627)NLEJ183546652 (DE-599)GBVNLZ183546652 DE-627 ger DE-627 rakwb eng Lack of adenylate and guanylate cyclases responsiveness to hormones in a spontaneous murine thyroid tumor 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Piot, J.-M. oth Jacquemin, C. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 1, Seite 357-366 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:1 pages:357-366 http://dx.doi.org/10.1016/0006-291X(80)90746-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 1 357-366 |
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(DE-627)NLEJ183546652 (DE-599)GBVNLZ183546652 DE-627 ger DE-627 rakwb eng Lack of adenylate and guanylate cyclases responsiveness to hormones in a spontaneous murine thyroid tumor 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Piot, J.-M. oth Jacquemin, C. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 1, Seite 357-366 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:1 pages:357-366 http://dx.doi.org/10.1016/0006-291X(80)90746-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 1 357-366 |
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(DE-627)NLEJ183546652 (DE-599)GBVNLZ183546652 DE-627 ger DE-627 rakwb eng Lack of adenylate and guanylate cyclases responsiveness to hormones in a spontaneous murine thyroid tumor 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Piot, J.-M. oth Jacquemin, C. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 1, Seite 357-366 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:1 pages:357-366 http://dx.doi.org/10.1016/0006-291X(80)90746-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 1 357-366 |
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(DE-627)NLEJ183546652 (DE-599)GBVNLZ183546652 DE-627 ger DE-627 rakwb eng Lack of adenylate and guanylate cyclases responsiveness to hormones in a spontaneous murine thyroid tumor 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Piot, J.-M. oth Jacquemin, C. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 1, Seite 357-366 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:1 pages:357-366 http://dx.doi.org/10.1016/0006-291X(80)90746-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 1 357-366 |
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(DE-627)NLEJ183546652 (DE-599)GBVNLZ183546652 DE-627 ger DE-627 rakwb eng Lack of adenylate and guanylate cyclases responsiveness to hormones in a spontaneous murine thyroid tumor 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Piot, J.-M. oth Jacquemin, C. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 95(1980), 1, Seite 357-366 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:95 year:1980 number:1 pages:357-366 http://dx.doi.org/10.1016/0006-291X(80)90746-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 95 1980 1 357-366 |
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Lack of adenylate and guanylate cyclases responsiveness to hormones in a spontaneous murine thyroid tumor |
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Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. |
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Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. |
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Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase. |
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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">NLEJ183546652</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706204557.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1980 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183546652</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183546652</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">Lack of adenylate and guanylate cyclases responsiveness to hormones in a spontaneous murine thyroid tumor</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1980</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">Animals with tumors were obtained from Dr. ZAJDELA and belong to sublines (XVIInc/Z/E) in which some individuals (TT) developed after 15 months thyroid tumors weighing between 150 and 1200 mg. Hyperplasia affects thyrocytes which do not present a follicular structure. The purpose of our work was to assay the action of various effectors on the adenylate and guanylate cyclase system in vitro. The following results have been obtained: the cyclic-AMP content of tumor tissue is not raised either by TSH or PGE"2. Nevertheless, TSH enhances the phosphatidylinositol phosphate turnover (phospholipid effect) as in normal tissue. This latter observation points at the existence of functional TSH receptors in tumor cells. The study of adenylate cyclase activity of the tumor homogenate shows the presence of this enzyme and its responsiveness to NaF and GppNHp. Unexpectedly, the cyclase is also sensitive to the stimulation by TSH.A tentative interpretation of these facts is that no component of the cyclase is missing, but that they are physically separated. The homogeneization allows the various components to interact productively.A parallel study was devoted to cyclic-GMP. Carbamylcholine fails to increase the cyclic-GMP content of the tumor tissue, whereas it has the described phospholipid effect on phosphatidylinositol. Nevertheless, there is no deficiency in the guanylate cyclase activity, since nitroprusside enhances strongly the cyclic-GMP content of the tumor.To conclude, the murine thyroid tumor presents a genetic alteration that results in the uncoupling of effector binding and catalytic stimulation of adenylate and guanylate cyclase.</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">Piot, J.-M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jacquemin, C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochemical and Biophysical Research Communications</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">95(1980), 1, Seite 357-366</subfield><subfield code="w">(DE-627)NLEJ176855645</subfield><subfield code="w">(DE-600)1461396-7</subfield><subfield code="x">0006-291X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:95</subfield><subfield code="g">year:1980</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:357-366</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0006-291X(80)90746-9</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">95</subfield><subfield code="j">1980</subfield><subfield code="e">1</subfield><subfield code="h">357-366</subfield></datafield></record></collection>
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