The influence of aminopterin administration on choline and formaldehyde oxidation by mouse liver
Identifieur interne : 001006 ( Main/Curation ); précédent : 001005; suivant : 001007The influence of aminopterin administration on choline and formaldehyde oxidation by mouse liver
Auteurs : Zelma Miller [États-Unis]Source :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1954.
English descriptors
- Teeft :
- Aminopterin, Aminopterin administration, Anaerobic, Anaerobic oxidation, Biochem, Biol, Chem, Choline, Choline oxidase, Choline oxidation, Cytochrome, Cytochrome oxidase, Dehydrogenase, Endogenous, Endogenous respiration, Federation proc, Ferricyanide, Formaldehyde, Formaldehyde oxidation, Homogenate, Liver choline oxidase, Liver homogenates, Malic, Malic dehydrogenase, Mouse liver homogenates, Nicotinamide, Normal aminopterin, Normal livers, Oxidase, Zelma miller.
Abstract
Abstract: Administration of aminopterin to mice causes a marked reduction in the oxidation of choline and formaldehyde by liver homogenates. The anaerobic oxidation of choline by ferricyanide is affected to only a slight degree.Diphosphopyridine nucleotide (DPN) increases the endogenous respiration of livers from normal and aminopterin-treated mice essentially the same amount. The DPN-stimulation of choline oxidation by livers from aminopterin-treated mice is far below the corresponding value in normal mice. The results suggest that ferricyanide relieves aminopterin inhibition either by non-enzymatic oxidation of DPN or of an unknown component which functions prior to the cytochrome oxidase system.Succinoxidase, cytochrome oxidase, and malic dehydrogenase are not influenced by aminopterin administration.
Url:
DOI: 10.1016/0003-9861(54)90048-X
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000489
- to stream Istex, to step Curation: Pour aller vers cette notice dans l'étape Curation :000488
- to stream Istex, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :000C39
- to stream Main, to step Merge: Pour aller vers cette notice dans l'étape Curation :001029
Links to Exploration step
ISTEX:AB6A62D8F261C3EB367806AC94039787FC11C623Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">The influence of aminopterin administration on choline and formaldehyde oxidation by mouse liver</title>
<author><name sortKey="Miller, Zelma" sort="Miller, Zelma" uniqKey="Miller Z" first="Zelma" last="Miller">Zelma Miller</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:AB6A62D8F261C3EB367806AC94039787FC11C623</idno>
<date when="1954" year="1954">1954</date>
<idno type="doi">10.1016/0003-9861(54)90048-X</idno>
<idno type="url">https://api.istex.fr/document/AB6A62D8F261C3EB367806AC94039787FC11C623/fulltext/pdf</idno>
<idno type="wicri:Area/Istex/Corpus">000489</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000489</idno>
<idno type="wicri:Area/Istex/Curation">000488</idno>
<idno type="wicri:Area/Istex/Checkpoint">000C39</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000C39</idno>
<idno type="wicri:doubleKey">0003-9861:1954:Miller Z:the:influence:of</idno>
<idno type="wicri:Area/Main/Merge">001029</idno>
<idno type="wicri:Area/Main/Curation">001006</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">The influence of aminopterin administration on choline and formaldehyde oxidation by mouse liver</title>
<author><name sortKey="Miller, Zelma" sort="Miller, Zelma" uniqKey="Miller Z" first="Zelma" last="Miller">Zelma Miller</name>
<affiliation wicri:level="3"><country xml:lang="fr">États-Unis</country>
<wicri:regionArea>From the Children's Cancer Research Foundation, the Children's Medical Center, and the Department of Pathology, Harvard Medical School, Boston</wicri:regionArea>
<placeName><settlement type="city">Boston</settlement>
<region type="state">Massachusetts</region>
</placeName>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series><title level="j">Archives of Biochemistry and Biophysics</title>
<title level="j" type="abbrev">YABBI</title>
<idno type="ISSN">0003-9861</idno>
<imprint><publisher>ELSEVIER</publisher>
<date type="published" when="1954">1954</date>
<biblScope unit="volume">50</biblScope>
<biblScope unit="issue">2</biblScope>
<biblScope unit="page" from="337">337</biblScope>
<biblScope unit="page" to="346">346</biblScope>
</imprint>
<idno type="ISSN">0003-9861</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><idno type="ISSN">0003-9861</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Aminopterin</term>
<term>Aminopterin administration</term>
<term>Anaerobic</term>
<term>Anaerobic oxidation</term>
<term>Biochem</term>
<term>Biol</term>
<term>Chem</term>
<term>Choline</term>
<term>Choline oxidase</term>
<term>Choline oxidation</term>
<term>Cytochrome</term>
<term>Cytochrome oxidase</term>
<term>Dehydrogenase</term>
<term>Endogenous</term>
<term>Endogenous respiration</term>
<term>Federation proc</term>
<term>Ferricyanide</term>
<term>Formaldehyde</term>
<term>Formaldehyde oxidation</term>
<term>Homogenate</term>
<term>Liver choline oxidase</term>
<term>Liver homogenates</term>
<term>Malic</term>
<term>Malic dehydrogenase</term>
<term>Mouse liver homogenates</term>
<term>Nicotinamide</term>
<term>Normal aminopterin</term>
<term>Normal livers</term>
<term>Oxidase</term>
<term>Zelma miller</term>
</keywords>
</textClass>
<langUsage><language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Abstract: Administration of aminopterin to mice causes a marked reduction in the oxidation of choline and formaldehyde by liver homogenates. The anaerobic oxidation of choline by ferricyanide is affected to only a slight degree.Diphosphopyridine nucleotide (DPN) increases the endogenous respiration of livers from normal and aminopterin-treated mice essentially the same amount. The DPN-stimulation of choline oxidation by livers from aminopterin-treated mice is far below the corresponding value in normal mice. The results suggest that ferricyanide relieves aminopterin inhibition either by non-enzymatic oxidation of DPN or of an unknown component which functions prior to the cytochrome oxidase system.Succinoxidase, cytochrome oxidase, and malic dehydrogenase are not influenced by aminopterin administration.</div>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Psychologie/explor/BernheimV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001006 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 001006 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Psychologie |area= BernheimV1 |flux= Main |étape= Curation |type= RBID |clé= ISTEX:AB6A62D8F261C3EB367806AC94039787FC11C623 |texte= The influence of aminopterin administration on choline and formaldehyde oxidation by mouse liver }}
This area was generated with Dilib version V0.6.33. |