Gastric metabolism of ethanol in Syrian golden hamster
Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian...
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E-Artikel |
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Englisch |
| Erschienen: |
1995 |
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| Umfang: |
5 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Digestive diseases and sciences - 1956, 40(1995) vom: Dez., Seite 2712-2716 |
| Übergeordnetes Werk: |
volume:40 ; year:1995 ; month:12 ; pages:2712-2716 ; extent:5 |
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| 520 | |a Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. | ||
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(DE-627)NLEJ197032729 DE-627 ger DE-627 rakwb eng Gastric metabolism of ethanol in Syrian golden hamster 1995 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. Springer Online Journal Archives 1860-2002 Batra, Subhash C. oth Haber, Paul S. oth Mirmiran-Yazdy, Fracp S. Ali A. oth Korsten, Mark A. oth Gentry, R. Thomas oth Lieber, Charles S. oth in Digestive diseases and sciences 1956 40(1995) vom: Dez., Seite 2712-2716 (DE-627)NLEJ18898948X (DE-600)2015102-0 1573-2568 nnns volume:40 year:1995 month:12 pages:2712-2716 extent:5 http://dx.doi.org/10.1007/BF02220464 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1995 12 2712-2716 5 |
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(DE-627)NLEJ197032729 DE-627 ger DE-627 rakwb eng Gastric metabolism of ethanol in Syrian golden hamster 1995 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. Springer Online Journal Archives 1860-2002 Batra, Subhash C. oth Haber, Paul S. oth Mirmiran-Yazdy, Fracp S. Ali A. oth Korsten, Mark A. oth Gentry, R. Thomas oth Lieber, Charles S. oth in Digestive diseases and sciences 1956 40(1995) vom: Dez., Seite 2712-2716 (DE-627)NLEJ18898948X (DE-600)2015102-0 1573-2568 nnns volume:40 year:1995 month:12 pages:2712-2716 extent:5 http://dx.doi.org/10.1007/BF02220464 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1995 12 2712-2716 5 |
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(DE-627)NLEJ197032729 DE-627 ger DE-627 rakwb eng Gastric metabolism of ethanol in Syrian golden hamster 1995 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. Springer Online Journal Archives 1860-2002 Batra, Subhash C. oth Haber, Paul S. oth Mirmiran-Yazdy, Fracp S. Ali A. oth Korsten, Mark A. oth Gentry, R. Thomas oth Lieber, Charles S. oth in Digestive diseases and sciences 1956 40(1995) vom: Dez., Seite 2712-2716 (DE-627)NLEJ18898948X (DE-600)2015102-0 1573-2568 nnns volume:40 year:1995 month:12 pages:2712-2716 extent:5 http://dx.doi.org/10.1007/BF02220464 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1995 12 2712-2716 5 |
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(DE-627)NLEJ197032729 DE-627 ger DE-627 rakwb eng Gastric metabolism of ethanol in Syrian golden hamster 1995 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. Springer Online Journal Archives 1860-2002 Batra, Subhash C. oth Haber, Paul S. oth Mirmiran-Yazdy, Fracp S. Ali A. oth Korsten, Mark A. oth Gentry, R. Thomas oth Lieber, Charles S. oth in Digestive diseases and sciences 1956 40(1995) vom: Dez., Seite 2712-2716 (DE-627)NLEJ18898948X (DE-600)2015102-0 1573-2568 nnns volume:40 year:1995 month:12 pages:2712-2716 extent:5 http://dx.doi.org/10.1007/BF02220464 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1995 12 2712-2716 5 |
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(DE-627)NLEJ197032729 DE-627 ger DE-627 rakwb eng Gastric metabolism of ethanol in Syrian golden hamster 1995 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. Springer Online Journal Archives 1860-2002 Batra, Subhash C. oth Haber, Paul S. oth Mirmiran-Yazdy, Fracp S. Ali A. oth Korsten, Mark A. oth Gentry, R. Thomas oth Lieber, Charles S. oth in Digestive diseases and sciences 1956 40(1995) vom: Dez., Seite 2712-2716 (DE-627)NLEJ18898948X (DE-600)2015102-0 1573-2568 nnns volume:40 year:1995 month:12 pages:2712-2716 extent:5 http://dx.doi.org/10.1007/BF02220464 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1995 12 2712-2716 5 |
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Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. |
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Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. |
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Abstract First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters. |
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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">NLEJ197032729</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230505191929.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070527s1995 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ197032729</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">Gastric metabolism of ethanol in Syrian golden hamster</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1995</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">5</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 First-pass metabolism (FPM) of orally ingested alcohol has been attributed to gastric alcohol dehydrogenase (ADH) activity in both humans and rats. To determine whether gastric alcohol dehydrogenase is essential for alcohol FPM, we sought a species lacking this enzyme. We found that Syrian golden hamsters have negligible gastric ADH yet alcohol FPM (265±25 mg ethanol/kg) was comparable to that of rats (251±31 mg/kg). To determine whether hamster gastric mucosal cells metabolize sufficient alcohol to account for this FPM, primary cultures were established, and these cells metabolized 1.99±0.84 μmol ethanol/106 cells/hr, an amount sufficient to account for the bulk of alcohol FPM. In contrast to alcohol dehydrogenase, catalase activity in hamster gastric mucosa (870±93 units/g tissue) was eightfold higher than in rat gastric mucosa (111±9 units/g tissue;P<0.0001). FPM in hamsters treated with 3-aminotriazole was reduced from 242±24 to 130±22 mg/kg (P<0.05) but was not reduced in rats. The results imply that catalase participates in gastric alcohol metabolism of hamsters.</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">Batra, Subhash C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Haber, Paul S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mirmiran-Yazdy, Fracp S. Ali A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Korsten, Mark A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gentry, R. Thomas</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lieber, Charles S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Digestive diseases and sciences</subfield><subfield code="d">1956</subfield><subfield code="g">40(1995) vom: Dez., Seite 2712-2716</subfield><subfield code="w">(DE-627)NLEJ18898948X</subfield><subfield code="w">(DE-600)2015102-0</subfield><subfield code="x">1573-2568</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:40</subfield><subfield code="g">year:1995</subfield><subfield code="g">month:12</subfield><subfield code="g">pages:2712-2716</subfield><subfield code="g">extent:5</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF02220464</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">40</subfield><subfield code="j">1995</subfield><subfield code="c">12</subfield><subfield code="h">2712-2716</subfield><subfield code="g">5</subfield></datafield></record></collection>
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