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

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) Vol. 14; no. 19; pp. 4273 - 4276
Main Authors: Kapke, Gordon, Davis, Leodis
Format: Journal Article
Language:English
Published: United States American Chemical Society 23-09-1975
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.
Bibliography:istex:1D22317CDE5367CE82581C66082285B8DEEDDB3E
ark:/67375/TPS-JHWFZRKL-B
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00690a020