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甲藻发光:一种NAD(P)H依赖性还原酶及其底物的纯化

Dinoflagellate luminescence: purification of a NAD(P)H-dependent reductase and of its substrate.

作者信息

Fresneau C, Hill M, Lescure N, Arrio B, Dupaix A, Volfin P

出版信息

Arch Biochem Biophys. 1986 Dec;251(2):495-503. doi: 10.1016/0003-9861(86)90357-7.

Abstract

The soluble enzymatic luminescent system of the dinoflagellate Pyrocystis lunula (luciferase-luciferin) is coupled with an enzymatic NAD(P)H-dependent reaction. The enzyme is a soluble reductase (Mr 47,000) which catalyzes, in the presence of NAD(P)H, the reduction of a molecule called P630. Reduced P630 has the same spectral characteristics as the purified luciferin. The luciferase can oxidize this reduced molecule with a light emission at 480 nm. These observations suggest that reduced P630 is a luciferin molecule. The oxidized form seems, in these conditions, to be the precursor of luciferin.

摘要

海洋发光甲藻(Pyrocystis lunula)的可溶性酶促发光系统(荧光素酶 - 荧光素)与一种依赖NAD(P)H的酶促反应相偶联。该酶是一种可溶性还原酶(分子量47,000),在NAD(P)H存在的情况下,它催化一种名为P630的分子的还原反应。还原态的P630具有与纯化后的荧光素相同的光谱特征。荧光素酶能够氧化这种还原态分子,并在480nm处发出光。这些观察结果表明,还原态的P630是荧光素分子。在这些条件下,氧化态似乎是荧光素的前体。

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