Optimized Spectrophotometric Assay for the Completely Activated Pyruvate Dehydrogenase Complex in Fibroblasts | Zendy

Marina A. Schwab | Zendy; Stefan Kölker | Zendy; Lambert P. van den Heuvel | Zendy; Sven W. Sauer | Zendy; Nicole I. Wolf | Zendy; D. Rating | Zendy; Georg F. Hoffmann | Zendy; Jan Smeitink | Zendy; Jürgen G. Okun | Zendy

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Optimized Spectrophotometric Assay for the Completely Activated Pyruvate Dehydrogenase Complex in Fibroblasts

Author(s) -

Marina A. Schwab,

Stefan Kölker,

Lambert P. van den Heuvel,

Sven W. Sauer,

Nicole I. Wolf,

D. Rating,

Georg F. Hoffmann,

Jan Smeitink,

Jürgen G. Okun

Publication year - 2004

Publication title -

clinical chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.705

H-Index - 218

eISSN - 1530-8561

pISSN - 0009-9147

DOI - 10.1373/clinchem.2004.033852

Subject(s) - dithiothreitol , pyruvate dehydrogenase complex , enzyme , chemistry , dehydrogenase , biochemistry , fibroblast , enzyme assay , microbiology and biotechnology , in vitro , biology

Analysis of the pyruvate dehydrogenase complex (PDHc) activity in human skin fibroblasts is hampered by low enzyme activity in the cells. The most commonly used radiochemical method detects the formation of (14)CO(2), an endproduct of the E1 component of PDHc, from [1-(14)C]pyruvate.

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