Expression and purification of active, stabilized trimethyllysine hydroxylase

•TMLH expressed in E. coli either alone, or as MBP fusion is mainly insoluble.•Co-expression of MBP–TMLH with chaperonins GroES/EL markedly improves solubility.•Purified MBP–TMLH is stable and functionally active. Trimethyllysine hydroxylase (TMLH) catalyses the first step in carnitine biosynthesis...

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Vydáno v:	Protein expression and purification Ročník 104; s. 1 - 6
Hlavní autoři:	Kazaks, Andris, Makrecka-Kuka, Marina, Kuka, Janis, Voronkova, Tatyana, Akopjana, Inara, Grinberga, Solveiga, Pugovics, Osvalds, Tars, Kaspars
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Elsevier Inc 01.12.2014
Témata:	Carnitine Carnitine - biosynthesis Chaperonins - genetics Chaperonins GroES/EL Enzyme Activation Escherichia coli gamma-Butyrobetaine Dioxygenase - metabolism Maltose-binding protein Maltose-Binding Proteins - genetics Mixed Function Oxygenases - genetics Mixed Function Oxygenases - isolation & purification Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - isolation & purification Trimethyllysine hydroxylase Chaperonins GroES/EL Maltose-binding protein Trimethyllysine hydroxylase Carnitine
ISSN:	1046-5928, 1096-0279, 1096-0279
On-line přístup:	Získat plný text
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