Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean
Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1974 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Archives of Biochemistry and Biophysics - Amsterdam : Elsevier, 164(1974), 1, Seite 95-105 |
| Übergeordnetes Werk: |
volume:164 ; year:1974 ; number:1 ; pages:95-105 |
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| 245 | 1 | 0 | |a Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean |
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| 520 | |a Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. | ||
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(DE-627)NLEJ183394429 (DE-599)GBVNLZ183394429 DE-627 ger DE-627 rakwb eng Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Gilchrist, D.G. oth Kosuge, T. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 164(1974), 1, Seite 95-105 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:164 year:1974 number:1 pages:95-105 http://dx.doi.org/10.1016/0003-9861(74)90011-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 164 1974 1 95-105 |
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(DE-627)NLEJ183394429 (DE-599)GBVNLZ183394429 DE-627 ger DE-627 rakwb eng Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Gilchrist, D.G. oth Kosuge, T. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 164(1974), 1, Seite 95-105 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:164 year:1974 number:1 pages:95-105 http://dx.doi.org/10.1016/0003-9861(74)90011-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 164 1974 1 95-105 |
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(DE-627)NLEJ183394429 (DE-599)GBVNLZ183394429 DE-627 ger DE-627 rakwb eng Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Gilchrist, D.G. oth Kosuge, T. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 164(1974), 1, Seite 95-105 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:164 year:1974 number:1 pages:95-105 http://dx.doi.org/10.1016/0003-9861(74)90011-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 164 1974 1 95-105 |
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(DE-627)NLEJ183394429 (DE-599)GBVNLZ183394429 DE-627 ger DE-627 rakwb eng Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Gilchrist, D.G. oth Kosuge, T. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 164(1974), 1, Seite 95-105 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:164 year:1974 number:1 pages:95-105 http://dx.doi.org/10.1016/0003-9861(74)90011-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 164 1974 1 95-105 |
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(DE-627)NLEJ183394429 (DE-599)GBVNLZ183394429 DE-627 ger DE-627 rakwb eng Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Gilchrist, D.G. oth Kosuge, T. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 164(1974), 1, Seite 95-105 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:164 year:1974 number:1 pages:95-105 http://dx.doi.org/10.1016/0003-9861(74)90011-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 164 1974 1 95-105 |
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regulation of aromatic amino acid biosynthesis in higher plants - properties of an aromatic amino acid-sensitive chorismate mutase (cm-1) from mung bean |
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Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean |
| abstract |
Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. |
| abstractGer |
Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. |
| abstract_unstemmed |
Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis. |
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Gilchrist, D.G. Kosuge, T. |
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NLEJ177020539 |
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2024-07-05T21:46:26.508Z |
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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">NLEJ183394429</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706201936.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1974 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183394429</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183394429</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">Regulation of aromatic amino acid biosynthesis in higher plants - Properties of an aromatic amino acid-sensitive chorismate mutase (CM-1) from mung bean</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1974</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">Chorismate mutase CM-1, an isozyme that is inhibited by phenylalanine and tyrosine and activated by tryptophan was purified 1200-fold from etiolated mung bean seedlings with a final yield of 18-20%. Loss of activity was rapid in highly purified preparations but was reduced by the addition of bovine serum albumin. Enzyme activity was unaffected by thiol-alkylating agents, reducing agents, EDTA, or divalent cations.The enzyme displayed pH-sensitive, positive homotrophic cooperativity toward chorismate with greatest cooperativity at the pH optimum of the tryptophan-free enzyme (pH 7.2-7.4) and least cooperativity at the pH optimum of the enzyme fully activated with tryptophan (pH 7.0). Activation by tryptophan reduced the K"m for the enzyme, and modified the sigmoid substrate saturation kinetics to a rectangular hyperbola. Feedback inhibition by the end product amino acids phenylalanine and tyrosine was not additive but revealed heterotrophic cooperativity with chorismate. Tyrosine (K"i = 31 μM) was a slightly more effective inhibitor than phenylalanine (K"i = 37 μM) at 1 mm chorismate. Tryptophan at equimolar concentration antagonized the feedback inhibition by phenylalanine and tyrosine. The latter two, however, at higher concentrations reversed the tryptophan activation in a noncompetitive fashion with respect to either tryptophan or chorismate. The enzyme was responsive only to the l-isomers of the amino acids. The results indicate a primary role for chorismate mutase CM-1 from mung bean in the regulation of the synthesis of phenylalanine and tyrosine for protein synthesis.</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">Gilchrist, D.G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kosuge, T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Archives of Biochemistry and Biophysics</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">164(1974), 1, Seite 95-105</subfield><subfield code="w">(DE-627)NLEJ177020539</subfield><subfield code="w">(DE-600)1461378-5</subfield><subfield code="x">0003-9861</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:164</subfield><subfield code="g">year:1974</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:95-105</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0003-9861(74)90011-3</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">164</subfield><subfield code="j">1974</subfield><subfield code="e">1</subfield><subfield code="h">95-105</subfield></datafield></record></collection>
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7.3999805 |