Simultaneous single-step purification of thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri

Thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri were purified by ion-exchange chromatography to near homogeneity in a simultaneous, single-step procedure. The yield of both enzymes was greater than 80%. Thiolase was purified approximately 8-fold with sp act 1...

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Veröffentlicht in:	Analytical biochemistry 1984-01, Vol.141 (2), p.344-347
Hauptverfasser:	Sliwkowski, Mark X., Hartmanis, Maris G.N.
Format:	Artikel
Sprache:	eng
Schlagworte:	3-Hydroxyacyl CoA Dehydrogenases - isolation & purification 3-hydroxybutyryl-CoA dehydrogenase acetyl-CoA acetyltransferase Acetyl-CoA C-Acetyltransferase - isolation & purification Acetyltransferases - isolation & purification Amino Acids - analysis basic proteins Chemical Phenomena Chemistry Chromatography, Ion Exchange Clostridium - enzymology Clostridium kluyveri Electrophoresis, Polyacrylamide Gel fatty acid-producing bacteria ion-exchange chromatography Isoelectric Focusing protein purification thiolase
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Beschreibung
Zusammenfassung:	Thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri were purified by ion-exchange chromatography to near homogeneity in a simultaneous, single-step procedure. The yield of both enzymes was greater than 80%. Thiolase was purified approximately 8-fold with sp act 115 units/mg, whereas 3-hydroxybutyryl-CoA dehydrogenase was purified 14-fold with sp act 292 units/mg. Isoelectric points of the enzymes are 7.7 for thiolase and 7.8 for 3-hydroxybutyryl-CoA dehydrogenase. Milligram quantities of each of these enzymes are readily obtained from this fatty acid-producing organism.
ISSN:	0003-2697 1096-0309
DOI:	10.1016/0003-2697(84)90052-6