Sheep liver serine-threonine dehydratase. I. Purification and evidence for covalently linked α-ketobutyrate as its cofactor

L-Serine-threonine dehydratase (EC 4.2.1.16) from sheep liver has been obtained as a highly purified preparation as shown by ultracentrifuge studies and analytical disc gel electrophoresis. The dehydratase has a molecular weight of 98,000 +/- 10,000 and is composed of two nonidentical subunits with...

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Bibliographic Details
Published in:Biochemistry (Easton) 1975-09, Vol.14 (19), p.4273-4276
Main Authors: Kapke, Gordon, Davis, Leodis
Format: Article
Language:English
Subjects:
Animals
Butyrates - analysis
Chromatography, DEAE-Cellulose
Chromatography, Gel
Coenzymes - analysis
Hydro-Lyases - isolation & purification
Keto Acids
Liver - enzymology
Macromolecular Substances
Molecular Weight
Sheep
Threonine Dehydratase - analysis
Threonine Dehydratase - isolation & purification
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Summary:L-Serine-threonine dehydratase (EC 4.2.1.16) from sheep liver has been obtained as a highly purified preparation as shown by ultracentrifuge studies and analytical disc gel electrophoresis. The dehydratase has a molecular weight of 98,000 +/- 10,000 and is composed of two nonidentical subunits with molecular weights of 41,000 and 47,000. The 41,000 subunit is covalently linked to the carbonyl reagent-sensitive coenzyme which has been identified as alpha-ketobutyric acid.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00690a020