Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit
Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formatio...
Ausführliche Beschreibung
Autor*in: |
Goldin, E. [verfasserIn] Harel, S [verfasserIn] Tomer, A. [verfasserIn] |
---|
Format: |
E-Artikel |
---|
Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1987 |
---|
Schlagwörter: |
---|
Umfang: |
Online-Ressource |
---|
Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
---|---|
Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 48(1987), 3, Seite 0 |
Übergeordnetes Werk: |
volume:48 ; year:1987 ; number:3 ; pages:0 |
Links: |
---|
DOI / URN: |
10.1111/j.1471-4159.1987.tb05572.x |
---|
Katalog-ID: |
NLEJ240288750 |
---|
LEADER | 01000caa a22002652 4500 | ||
---|---|---|---|
001 | NLEJ240288750 | ||
003 | DE-627 | ||
005 | 20210707105701.0 | ||
007 | cr uuu---uuuuu | ||
008 | 120426s1987 xx |||||o 00| ||und c | ||
024 | 7 | |a 10.1111/j.1471-4159.1987.tb05572.x |2 doi | |
035 | |a (DE-627)NLEJ240288750 | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
100 | 1 | |a Goldin, E. |e verfasserin |4 aut | |
245 | 1 | 0 | |a Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit |
264 | 1 | |a Oxford, UK |b Blackwell Publishing Ltd |c 1987 | |
300 | |a Online-Ressource | ||
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 Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. | ||
533 | |d 2006 |f Blackwell Publishing Journal Backfiles 1879-2005 |7 |2006|||||||||| | ||
650 | 4 | |a Fetal brain development | |
700 | 1 | |a Harel, S |e verfasserin |4 aut | |
700 | 1 | |a Tomer, A. |e verfasserin |4 aut | |
700 | 1 | |a Yavin, E. |4 oth | |
773 | 0 | 8 | |i In |t Journal of neurochemistry |d Oxford : Wiley-Blackwell, 1956 |g 48(1987), 3, Seite 0 |h Online-Ressource |w (DE-627)NLEJ243927584 |w (DE-600)2020528-4 |x 1471-4159 |7 nnns |
773 | 1 | 8 | |g volume:48 |g year:1987 |g number:3 |g pages:0 |
856 | 4 | 0 | |u http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x |q text/html |x Verlag |z Deutschlandweit zugänglich |3 Volltext |
912 | |a GBV_USEFLAG_U | ||
912 | |a ZDB-1-DJB | ||
912 | |a GBV_NL_ARTICLE | ||
951 | |a AR | ||
952 | |d 48 |j 1987 |e 3 |h 0 |
author_variant |
e g eg s h sh a t at |
---|---|
matchkey_str |
article:14714159:1987----::rcioiaioiainyriadlcnarprtosrmomlnpae |
hierarchy_sort_str |
1987 |
publishDate |
1987 |
allfields |
10.1111/j.1471-4159.1987.tb05572.x doi (DE-627)NLEJ240288750 DE-627 ger DE-627 rakwb Goldin, E. verfasserin aut Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit Oxford, UK Blackwell Publishing Ltd 1987 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Fetal brain development Harel, S verfasserin aut Tomer, A. verfasserin aut Yavin, E. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 48(1987), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:48 year:1987 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 48 1987 3 0 |
spelling |
10.1111/j.1471-4159.1987.tb05572.x doi (DE-627)NLEJ240288750 DE-627 ger DE-627 rakwb Goldin, E. verfasserin aut Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit Oxford, UK Blackwell Publishing Ltd 1987 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Fetal brain development Harel, S verfasserin aut Tomer, A. verfasserin aut Yavin, E. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 48(1987), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:48 year:1987 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 48 1987 3 0 |
allfields_unstemmed |
10.1111/j.1471-4159.1987.tb05572.x doi (DE-627)NLEJ240288750 DE-627 ger DE-627 rakwb Goldin, E. verfasserin aut Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit Oxford, UK Blackwell Publishing Ltd 1987 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Fetal brain development Harel, S verfasserin aut Tomer, A. verfasserin aut Yavin, E. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 48(1987), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:48 year:1987 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 48 1987 3 0 |
allfieldsGer |
10.1111/j.1471-4159.1987.tb05572.x doi (DE-627)NLEJ240288750 DE-627 ger DE-627 rakwb Goldin, E. verfasserin aut Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit Oxford, UK Blackwell Publishing Ltd 1987 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Fetal brain development Harel, S verfasserin aut Tomer, A. verfasserin aut Yavin, E. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 48(1987), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:48 year:1987 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 48 1987 3 0 |
allfieldsSound |
10.1111/j.1471-4159.1987.tb05572.x doi (DE-627)NLEJ240288750 DE-627 ger DE-627 rakwb Goldin, E. verfasserin aut Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit Oxford, UK Blackwell Publishing Ltd 1987 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Fetal brain development Harel, S verfasserin aut Tomer, A. verfasserin aut Yavin, E. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 48(1987), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:48 year:1987 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 48 1987 3 0 |
source |
In Journal of neurochemistry 48(1987), 3, Seite 0 volume:48 year:1987 number:3 pages:0 |
sourceStr |
In Journal of neurochemistry 48(1987), 3, Seite 0 volume:48 year:1987 number:3 pages:0 |
format_phy_str_mv |
Article |
institution |
findex.gbv.de |
topic_facet |
Fetal brain development |
isfreeaccess_bool |
false |
container_title |
Journal of neurochemistry |
authorswithroles_txt_mv |
Goldin, E. @@aut@@ Harel, S @@aut@@ Tomer, A. @@aut@@ Yavin, E. @@oth@@ |
publishDateDaySort_date |
1987-01-01T00:00:00Z |
hierarchy_top_id |
NLEJ243927584 |
id |
NLEJ240288750 |
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">NLEJ240288750</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707105701.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1987 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1471-4159.1987.tb05572.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240288750</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="100" ind1="1" ind2=" "><subfield code="a">Goldin, E.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1987</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</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: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Fetal brain development</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Harel, S</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tomer, A.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yavin, E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of neurochemistry</subfield><subfield code="d">Oxford : Wiley-Blackwell, 1956</subfield><subfield code="g">48(1987), 3, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927584</subfield><subfield code="w">(DE-600)2020528-4</subfield><subfield code="x">1471-4159</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:48</subfield><subfield code="g">year:1987</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</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-DJB</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">48</subfield><subfield code="j">1987</subfield><subfield code="e">3</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
series2 |
Blackwell Publishing Journal Backfiles 1879-2005 |
author |
Goldin, E. |
spellingShingle |
Goldin, E. misc Fetal brain development Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit |
authorStr |
Goldin, E. |
ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ243927584 |
format |
electronic Article |
delete_txt_mv |
keep |
author_role |
aut aut aut |
collection |
NL |
publishPlace |
Oxford, UK |
remote_str |
true |
illustrated |
Not Illustrated |
issn |
1471-4159 |
topic_title |
Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit Fetal brain development |
publisher |
Blackwell Publishing Ltd |
publisherStr |
Blackwell Publishing Ltd |
topic |
misc Fetal brain development |
topic_unstemmed |
misc Fetal brain development |
topic_browse |
misc Fetal brain development |
format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
format_main_str_mv |
Text Zeitschrift/Artikel |
carriertype_str_mv |
zu |
author2_variant |
e y ey |
hierarchy_parent_title |
Journal of neurochemistry |
hierarchy_parent_id |
NLEJ243927584 |
hierarchy_top_title |
Journal of neurochemistry |
isfreeaccess_txt |
false |
familylinks_str_mv |
(DE-627)NLEJ243927584 (DE-600)2020528-4 |
title |
Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit |
ctrlnum |
(DE-627)NLEJ240288750 |
title_full |
Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit |
author_sort |
Goldin, E. |
journal |
Journal of neurochemistry |
journalStr |
Journal of neurochemistry |
isOA_bool |
false |
recordtype |
marc |
publishDateSort |
1987 |
contenttype_str_mv |
zzz |
container_start_page |
0 |
author_browse |
Goldin, E. Harel, S Tomer, A. |
container_volume |
48 |
physical |
Online-Ressource |
format_se |
Elektronische Aufsätze |
author-letter |
Goldin, E. |
doi_str_mv |
10.1111/j.1471-4159.1987.tb05572.x |
author2-role |
verfasserin |
title_sort |
arachidonic acid oxidation by brain and placenta preparations from normal and placental insufficient fetal rabbit |
title_auth |
Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit |
abstract |
Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. |
abstractGer |
Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. |
abstract_unstemmed |
Abstract: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron. |
collection_details |
GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE |
container_issue |
3 |
title_short |
Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit |
url |
http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x |
remote_bool |
true |
author2 |
Harel, S Tomer, A. Yavin, E. |
author2Str |
Harel, S Tomer, A. Yavin, E. |
ppnlink |
NLEJ243927584 |
mediatype_str_mv |
z |
isOA_txt |
false |
hochschulschrift_bool |
false |
author2_role |
oth |
doi_str |
10.1111/j.1471-4159.1987.tb05572.x |
up_date |
2024-07-06T09:36:00.047Z |
_version_ |
1803821839860891648 |
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">NLEJ240288750</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707105701.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1987 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1471-4159.1987.tb05572.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240288750</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="100" ind1="1" ind2=" "><subfield code="a">Goldin, E.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Arachidonic Acid Oxidation by Brain and Placenta Preparations from Normal and Placental Insufficient Fetal Rabbit</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1987</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</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: Cytosolic (100,000 g) fractions of fetal rabbit brain and placenta tissue convert [1–14C]arachidonic acid into several oxidation products identified with the lipoxygenase [12-hydroxyeicosatetraenoic acid (12-HETE) and 15-HETE] and cyclooxygenase [prostaglandin E2 (PGE2)] pathways. Formation of 12-HETE and 15-HETE by fetal brain is time-dependent, reaching a plateau after 40 min and is linear with protein concentration. An apparent affinity constant of 0.06 mM and a Vmax of 0.1 μmol/h/g wet weight are presumably responsible for the excessive accumulation of 12-HETE and 15-HETE in comparison to PGE2 (Km=0.5 mM). The latter is synthesized by the placenta particulate fraction but almost exclusively by the brain cytosol. Compared to brain, the activity of the placenta tissue is exceedingly higher and in addition to 12-HETE and 15-HETE there is a substantial formation of 12–l-hydroxyheptadecatrienic acid. Formation of 12-HETE and 15-HETE at 21 days is as effective as at 31 days gestation and is strongly inhibited by nordihydroguaiaretic acid (93%), BW755c (99%), and AA861 (84%) but not by indomethacin. Placenta and brain tissues of intrauterine growth retarded fetuses after ligation of placental blood vessels fail to convert arachidonic acid into other eicosanoids. Loss of enzymatic activity also observed in normal tissue after prolonged storage cannot be restored by the addition of several SH agents, ascorbate, or ferric iron.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Fetal brain development</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Harel, S</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tomer, A.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yavin, E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of neurochemistry</subfield><subfield code="d">Oxford : Wiley-Blackwell, 1956</subfield><subfield code="g">48(1987), 3, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927584</subfield><subfield code="w">(DE-600)2020528-4</subfield><subfield code="x">1471-4159</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:48</subfield><subfield code="g">year:1987</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1471-4159.1987.tb05572.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</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-DJB</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">48</subfield><subfield code="j">1987</subfield><subfield code="e">3</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
score |
7.400137 |