A nonradioactive assay for N super(5)-methyltetrahydrofolate-homocysteine methyltransferase (methionine synthase) based on o-phthaldialdehyde derivatization of methionine and fluorescence detection

The enzyme N super(5)-methyltetrahydrofolate-homocysteine methyltransferase (methionine synthase, EC 2.1.1.13) catalyzes the conversion of homocysteine to methionine in the presence of a reducing system. N super(5)-Methyltetrahydrofolate serves as a methyl donor in this reaction. An assay for the en...

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Bibliographic Details
Published inAnalytical biochemistry Vol. 199; no. 1; pp. 112 - 118
Main Authors Garras, A, Djurhuus, R, Christensen, B, Lillehaug, J R, Ueland, P M
Format Journal Article
LanguageEnglish
Published 01.01.1991
Subjects
methionine
o-phthaldialdehyde
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Summary:The enzyme N super(5)-methyltetrahydrofolate-homocysteine methyltransferase (methionine synthase, EC 2.1.1.13) catalyzes the conversion of homocysteine to methionine in the presence of a reducing system. N super(5)-Methyltetrahydrofolate serves as a methyl donor in this reaction. An assay for the enzyme is described, which is based on methionine quantitation by o-phthaldialdehyde (OPA) derivatization and reversed-phase liquid chromatography. This nonradioactive assay for methionine synthase was evaluated by comparison with a conventional method based on isolation of radioactive methionine by anion-exchange chromatography and by determination of enzyme activity in extract from cultured cells and liver.
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ISSN:0003-2697