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PMID: 6712627 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The purification and properties of ox liver short-chain acyl-CoA dehydrogenase.

The Biochemical journal ·Vol. 218 ·No. 2 ·1984-03-01 ·Pages 511-20

Shaw L, Engel PC

Abstract

The FAD-containing short-chain acyl-CoA dehydrogenase was purified from ox liver mitochondria by using (NH4)2SO4 fractionation, DEAE-Sephadex A-50 and chromatofocusing on PBE 94 resin. The enzyme is a tetramer, with a native Mr of approx. 162 000 and a subunit Mr of 41 000. Short-chain acyl-CoA dehydrogenases are usually isolated in a green form. The chromatofocusing step in the purification presented here partially resolved the enzyme into a green form and a yellow form. In the dye-mediated assay system, the enzyme exhibited optimal activity towards 50 microM-butyryl-CoA at pH 7.1. Kinetic parameters were also determined for a number of other straight-chain acyl-CoA substrates. The u.v.- and visible-absorption characteristics of the native forms of the enzyme are described, together with complexes formed by addition of butyryl-CoA, acetoacetyl-CoA and CoA persulphide.

MeSH Terms
Acetyl Coenzyme A/analogs & derivatives,metabolism Acyl Coenzyme A/metabolism Acyl-CoA Dehydrogenase Acyl-CoA Dehydrogenases/isolation & purification,metabolism Animals Cattle Chromatography, Ion Exchange Hydrogen-Ion Concentration Kinetics Male Mitochondria, Liver/enzymology Spectrophotometry Substrate Specificity
Chemicals
Acyl Coenzyme A acetoacetyl CoA butyryl-coenzyme A Acetyl Coenzyme A Acyl-CoA Dehydrogenases Acyl-CoA Dehydrogenase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Shaw L
Engel P C
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30 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2180511
Published
1984-03-01
Pages
511-20
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1153367
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2180511 PMC Full Text View journal details
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