Rotating disc electrode characterization of immobilized glucose oxidase
The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-elect...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1991 |
|---|
| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Analytical Biochemistry - Amsterdam : Elsevier, 195(1991), 2, Seite 358-363 |
| Übergeordnetes Werk: |
volume:195 ; year:1991 ; number:2 ; pages:358-363 |
| Links: |
|---|
| Katalog-ID: |
NLEJ184041295 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ184041295 | ||
| 003 | DE-627 | ||
| 005 | 20210706221115.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 070506s1991 xx |||||o 00| ||eng c | ||
| 035 | |a (DE-627)NLEJ184041295 | ||
| 035 | |a (DE-599)GBVNLZ184041295 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 245 | 1 | 0 | |a Rotating disc electrode characterization of immobilized glucose oxidase |
| 264 | 1 | |c 1991 | |
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. | ||
| 533 | |f Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 | ||
| 700 | 1 | |a Mikkelsen, S.R. |4 oth | |
| 700 | 1 | |a Lennox, R.B. |4 oth | |
| 773 | 0 | 8 | |i in |t Analytical Biochemistry |d Amsterdam : Elsevier |g 195(1991), 2, Seite 358-363 |w (DE-627)NLEJ17685830X |w (DE-600)1461105-3 |x 0003-2697 |7 nnns |
| 773 | 1 | 8 | |g volume:195 |g year:1991 |g number:2 |g pages:358-363 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1016/0003-2697(91)90341-P |
| 912 | |a GBV_USEFLAG_H | ||
| 912 | |a ZDB-1-SDJ | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 195 |j 1991 |e 2 |h 358-363 | ||
| matchkey_str |
article:00032697:1991----::oaigiclcrdcaatrztooimblz |
|---|---|
| hierarchy_sort_str |
1991 |
| publishDate |
1991 |
| allfields |
(DE-627)NLEJ184041295 (DE-599)GBVNLZ184041295 DE-627 ger DE-627 rakwb eng Rotating disc electrode characterization of immobilized glucose oxidase 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mikkelsen, S.R. oth Lennox, R.B. oth in Analytical Biochemistry Amsterdam : Elsevier 195(1991), 2, Seite 358-363 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:195 year:1991 number:2 pages:358-363 http://dx.doi.org/10.1016/0003-2697(91)90341-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 195 1991 2 358-363 |
| spelling |
(DE-627)NLEJ184041295 (DE-599)GBVNLZ184041295 DE-627 ger DE-627 rakwb eng Rotating disc electrode characterization of immobilized glucose oxidase 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mikkelsen, S.R. oth Lennox, R.B. oth in Analytical Biochemistry Amsterdam : Elsevier 195(1991), 2, Seite 358-363 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:195 year:1991 number:2 pages:358-363 http://dx.doi.org/10.1016/0003-2697(91)90341-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 195 1991 2 358-363 |
| allfields_unstemmed |
(DE-627)NLEJ184041295 (DE-599)GBVNLZ184041295 DE-627 ger DE-627 rakwb eng Rotating disc electrode characterization of immobilized glucose oxidase 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mikkelsen, S.R. oth Lennox, R.B. oth in Analytical Biochemistry Amsterdam : Elsevier 195(1991), 2, Seite 358-363 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:195 year:1991 number:2 pages:358-363 http://dx.doi.org/10.1016/0003-2697(91)90341-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 195 1991 2 358-363 |
| allfieldsGer |
(DE-627)NLEJ184041295 (DE-599)GBVNLZ184041295 DE-627 ger DE-627 rakwb eng Rotating disc electrode characterization of immobilized glucose oxidase 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mikkelsen, S.R. oth Lennox, R.B. oth in Analytical Biochemistry Amsterdam : Elsevier 195(1991), 2, Seite 358-363 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:195 year:1991 number:2 pages:358-363 http://dx.doi.org/10.1016/0003-2697(91)90341-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 195 1991 2 358-363 |
| allfieldsSound |
(DE-627)NLEJ184041295 (DE-599)GBVNLZ184041295 DE-627 ger DE-627 rakwb eng Rotating disc electrode characterization of immobilized glucose oxidase 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mikkelsen, S.R. oth Lennox, R.B. oth in Analytical Biochemistry Amsterdam : Elsevier 195(1991), 2, Seite 358-363 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:195 year:1991 number:2 pages:358-363 http://dx.doi.org/10.1016/0003-2697(91)90341-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 195 1991 2 358-363 |
| language |
English |
| source |
in Analytical Biochemistry 195(1991), 2, Seite 358-363 volume:195 year:1991 number:2 pages:358-363 |
| sourceStr |
in Analytical Biochemistry 195(1991), 2, Seite 358-363 volume:195 year:1991 number:2 pages:358-363 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Analytical Biochemistry |
| authorswithroles_txt_mv |
Mikkelsen, S.R. @@oth@@ Lennox, R.B. @@oth@@ |
| publishDateDaySort_date |
1991-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ17685830X |
| id |
NLEJ184041295 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ184041295</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706221115.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1991 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ184041295</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ184041295</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">Rotating disc electrode characterization of immobilized glucose oxidase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1991</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">The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design.</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">Mikkelsen, S.R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lennox, R.B.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Analytical Biochemistry</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">195(1991), 2, Seite 358-363</subfield><subfield code="w">(DE-627)NLEJ17685830X</subfield><subfield code="w">(DE-600)1461105-3</subfield><subfield code="x">0003-2697</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:195</subfield><subfield code="g">year:1991</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:358-363</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0003-2697(91)90341-P</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">195</subfield><subfield code="j">1991</subfield><subfield code="e">2</subfield><subfield code="h">358-363</subfield></datafield></record></collection>
|
| series2 |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ17685830X |
| format |
electronic Article |
| delete_txt_mv |
keep |
| collection |
NL |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
0003-2697 |
| topic_title |
Rotating disc electrode characterization of immobilized glucose oxidase |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
s m sm r l rl |
| hierarchy_parent_title |
Analytical Biochemistry |
| hierarchy_parent_id |
NLEJ17685830X |
| hierarchy_top_title |
Analytical Biochemistry |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ17685830X (DE-600)1461105-3 |
| title |
Rotating disc electrode characterization of immobilized glucose oxidase |
| spellingShingle |
Rotating disc electrode characterization of immobilized glucose oxidase |
| ctrlnum |
(DE-627)NLEJ184041295 (DE-599)GBVNLZ184041295 |
| title_full |
Rotating disc electrode characterization of immobilized glucose oxidase |
| journal |
Analytical Biochemistry |
| journalStr |
Analytical Biochemistry |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1991 |
| contenttype_str_mv |
zzz |
| container_start_page |
358 |
| container_volume |
195 |
| format_se |
Elektronische Aufsätze |
| title_sort |
rotating disc electrode characterization of immobilized glucose oxidase |
| title_auth |
Rotating disc electrode characterization of immobilized glucose oxidase |
| abstract |
The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. |
| abstractGer |
The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. |
| abstract_unstemmed |
The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design. |
| collection_details |
GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE |
| container_issue |
2 |
| title_short |
Rotating disc electrode characterization of immobilized glucose oxidase |
| url |
http://dx.doi.org/10.1016/0003-2697(91)90341-P |
| remote_bool |
true |
| author2 |
Mikkelsen, S.R. Lennox, R.B. |
| author2Str |
Mikkelsen, S.R. Lennox, R.B. |
| ppnlink |
NLEJ17685830X |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth |
| up_date |
2024-07-06T00:00:14.801Z |
| _version_ |
1803785616546070528 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ184041295</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706221115.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1991 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ184041295</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ184041295</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">Rotating disc electrode characterization of immobilized glucose oxidase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1991</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">The kinetic properties of glucose oxidase (EC 1.1.3.4) which has been covalently immobilized to a rotating glassy carbon electrode surface have been investigated. Analysis of the rotation rate dependence of the hydrogen peroxide-derived current suggests that oxygen mass transport to the enzyme-electrode surface is rate controlling at low rotation rates. Only as the diffusion layer approaches zero thickness (i.e., infinitely fast rotation rate) does mass transport become unimportant. A diffusion-free glucose K"m for air-saturated buffer is found to be 66 mM using this methodology. The importance of mass transport restrictions in two-substrate enzymes such as glucose oxidase is discussed in the context of biosensor design.</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">Mikkelsen, S.R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lennox, R.B.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Analytical Biochemistry</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">195(1991), 2, Seite 358-363</subfield><subfield code="w">(DE-627)NLEJ17685830X</subfield><subfield code="w">(DE-600)1461105-3</subfield><subfield code="x">0003-2697</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:195</subfield><subfield code="g">year:1991</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:358-363</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0003-2697(91)90341-P</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">195</subfield><subfield code="j">1991</subfield><subfield code="e">2</subfield><subfield code="h">358-363</subfield></datafield></record></collection>
|
| score |
7.401742 |