Solubilization and purification of aldehyde‐generating fatty acyl‐CoA reductase from green alga Botryococcus braunii

FEBS Letters

Kolattukudy, Pappachan E.¹  Wang, Xing¹ 

[1] Neurobiotechnology Center, the Ohio State University, 206 Rightmire Hall, 1060 Carmack Road, Columbus, OH 43210, USA

关键词: Acyl-CoA reductase;    Purification;    N-terminal sequence;    Hydrocarbon;    Aldehyde;    Botryococcus braunii;   

DOI  :  10.1016/0014-5793(95)00781-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Membrane-bound fatty acyl-CoA reductase from the green alga Botryococcus braunii has been solubilized from the microsomal preparation by 0.1% octyl β-glucoside and purified to near homogeneity by Blue A agarose and palmitoyl-CoA agarose affinity column chromatography. The molecular mass of the enzyme was estimated by SDS-PAGE to be 35 kDa. The enzyme generates fatty aldehyde by reduction of fatty acyl-CoA with NADH as the reductant. The N-terminal amino acid sequence of this protein that represents the first eucaryotic aldehyde-generating reductase to be purified shows high homology with the N-terminus of fatty acid reductase from bacteria.

【 授权许可】

Unknown