Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes
Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwar...
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1997 |
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| Umfang: |
14 |
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Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: The journal of membrane biology - 1969, 155(1997) vom: Feb., Seite 143 -156 |
| Übergeordnetes Werk: |
volume:155 ; year:1997 ; month:02 ; pages:143 -156 ; extent:14 |
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NLEJ207049408 |
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| 245 | 1 | 0 | |a Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes |
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| 520 | |a Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. | ||
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| 700 | 1 | |a Iino, M. |4 oth | |
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| 700 | 1 | |a Ozawa, S. |4 oth | |
| 700 | 1 | |a Kidokoro, Y. |4 oth | |
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(DE-627)NLEJ207049408 DE-627 ger DE-627 rakwb eng Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes 1997 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. Springer Online Journal Archives 1860-2002 Iino, M. oth Ciani, S. oth Tsuzuki, K. oth Ozawa, S. oth Kidokoro, Y. oth in The journal of membrane biology 1969 155(1997) vom: Feb., Seite 143 -156 (DE-627)NLEJ18899419X (DE-600)1459323-3 1432-1424 nnns volume:155 year:1997 month:02 pages:143 -156 extent:14 http://dx.doi.org/10.1007/s002329900166 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 155 1997 2 143 -156 14 |
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(DE-627)NLEJ207049408 DE-627 ger DE-627 rakwb eng Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes 1997 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. Springer Online Journal Archives 1860-2002 Iino, M. oth Ciani, S. oth Tsuzuki, K. oth Ozawa, S. oth Kidokoro, Y. oth in The journal of membrane biology 1969 155(1997) vom: Feb., Seite 143 -156 (DE-627)NLEJ18899419X (DE-600)1459323-3 1432-1424 nnns volume:155 year:1997 month:02 pages:143 -156 extent:14 http://dx.doi.org/10.1007/s002329900166 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 155 1997 2 143 -156 14 |
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(DE-627)NLEJ207049408 DE-627 ger DE-627 rakwb eng Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes 1997 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. Springer Online Journal Archives 1860-2002 Iino, M. oth Ciani, S. oth Tsuzuki, K. oth Ozawa, S. oth Kidokoro, Y. oth in The journal of membrane biology 1969 155(1997) vom: Feb., Seite 143 -156 (DE-627)NLEJ18899419X (DE-600)1459323-3 1432-1424 nnns volume:155 year:1997 month:02 pages:143 -156 extent:14 http://dx.doi.org/10.1007/s002329900166 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 155 1997 2 143 -156 14 |
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(DE-627)NLEJ207049408 DE-627 ger DE-627 rakwb eng Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes 1997 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. Springer Online Journal Archives 1860-2002 Iino, M. oth Ciani, S. oth Tsuzuki, K. oth Ozawa, S. oth Kidokoro, Y. oth in The journal of membrane biology 1969 155(1997) vom: Feb., Seite 143 -156 (DE-627)NLEJ18899419X (DE-600)1459323-3 1432-1424 nnns volume:155 year:1997 month:02 pages:143 -156 extent:14 http://dx.doi.org/10.1007/s002329900166 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 155 1997 2 143 -156 14 |
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(DE-627)NLEJ207049408 DE-627 ger DE-627 rakwb eng Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes 1997 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. Springer Online Journal Archives 1860-2002 Iino, M. oth Ciani, S. oth Tsuzuki, K. oth Ozawa, S. oth Kidokoro, Y. oth in The journal of membrane biology 1969 155(1997) vom: Feb., Seite 143 -156 (DE-627)NLEJ18899419X (DE-600)1459323-3 1432-1424 nnns volume:155 year:1997 month:02 pages:143 -156 extent:14 http://dx.doi.org/10.1007/s002329900166 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 155 1997 2 143 -156 14 |
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Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. 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Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes |
| abstract |
Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. |
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Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. |
| abstract_unstemmed |
Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site. |
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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">NLEJ207049408</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706220153.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s1997 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ207049408</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">Permeation Properties of Na+ and Ca2+ Ions through the Mouse ε2/ζ1 NMDA Receptor Channel Expressed in Xenopus Oocytes</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1997</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">14</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">Abstract. Ion permeation properties of the mouse e2/ζ1 NMDA receptor channel expressed in Xenopus oocytes were studied using the outside-out patch-clamp technique. In symmetrical Na+ solutions, the single-channel I-V relations were almost linear at low electrolyte concentrations, but rectified inwardly for Na+ concentrations above 50 mm. In symmetrical Na+ solutions, the ``zero-current conductance'' increased with Na+ concentration and saturated according to a hyperbolic curve, the half-maximal saturating activity, K M (Na), being 14.2 mm and the maximal conductance, G max(Na), 53.9 pS. When Ca2+ was present with Na+ in the external solution, the single-channel current was lower than in pure Na+, although the reversal potential indicated a higher permeability for Ca2+ than for Na+. Using ion activities, PCa/PNa was found to be about 17. The I-V data were fitted with a model based on the Eyring's rate theory, assuming a one-ion pore with three energy barriers and two sites. The K M (Ca) and G max (Ca) were 76.5 μm and 21.2 pS, respectively. According to the estimated rate constants, K M for Ca2+ is mainly determined by the binding strength of a site located 80% away from the channel opening at the external membrane-solution interface, a position similar to that postulated previously for the Mg2+ blocking site.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Iino, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ciani, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tsuzuki, K.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ozawa, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kidokoro, Y.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">The journal of membrane biology</subfield><subfield code="d">1969</subfield><subfield code="g">155(1997) vom: Feb., Seite 143 -156</subfield><subfield code="w">(DE-627)NLEJ18899419X</subfield><subfield code="w">(DE-600)1459323-3</subfield><subfield code="x">1432-1424</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:155</subfield><subfield code="g">year:1997</subfield><subfield code="g">month:02</subfield><subfield code="g">pages:143 -156</subfield><subfield code="g">extent:14</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/s002329900166</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</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">155</subfield><subfield code="j">1997</subfield><subfield code="c">2</subfield><subfield code="h">143 -156</subfield><subfield code="g">14</subfield></datafield></record></collection>
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