The influence of aminopterin administration on choline and formaldehyde oxidation by mouse liver
Identifieur interne : 000C39 ( Istex/Checkpoint ); précédent : 000C38; suivant : 000C40The 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
Affiliations:
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ISTEX:AB6A62D8F261C3EB367806AC94039787FC11C623Le document en format XML
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<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>
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<series><title level="j">Archives of Biochemistry and Biophysics</title>
<title level="j" type="abbrev">YABBI</title>
<idno type="ISSN">0003-9861</idno>
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<date type="published" when="1954">1954</date>
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<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>
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<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>
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