脂质体细胞色素P-450 LM2的迁移性和簇状组织:饱和转移EPR研究。

Acta biologica et medica Germanica Pub Date : 1982-01-01
D Schwarz, J Pirrwitz, M J Coon, K Ruckpaul
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引用次数: 0

摘要

利用饱和转移EPR光谱研究了兔肝微粒体中电泳均相细胞色素P-450 LM2在缓冲液和磷脂囊泡中的旋转扩散。用马来酰亚胺自旋标记选择性地修饰酶的巯基。细胞色素P-450在缓冲溶液中旋转的有效旋转相关时间为220 ns,这与纯化的游离酶以低聚体(6-8个单体)聚集的形式出现的事实是一致的。此外,这些星团几乎是各向同性旋转的,因此在第一个近似上是球形的。有效相关时间约为180微秒,观察到强固定化,从而证明膜内蛋白质聚集。光谱的各向异性特征表明团簇的非球形和/或各向异性旋转运动。结果与微粒体形式细胞色素P-450的相应数据进行了比较。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Mobility and clusterlike organization of liposomal cytochrome P-450 LM2: saturation transfer EPR studies.

Rotational diffusion of the electrophoretically homogenenous isozyme cytochrome P-450 LM2 from rabbit liver microsomes has been studied in buffer solution and in phospholipid vesicles by means of saturation transfer EPR spectroscopy. Sulfhydryl groups of the enzyme were selectively modified using a maleimide spin label. The effective rotational correlation time of 220 ns for the rotation of cytochrome P-450 in buffer solution is consistent with the fact that the purified free enzyme occurs as an oligomeric (6-8 monomers) aggregate. Further, the clusters rotate almost isotropically and therefore are in a first approximation spherically shaped. The effective correlation time of about 180 microseconds observed strong immobilization thus evidencing protein aggregation within the membrane. The anisotropic character of the spectra indicates a nonspherical shape and/or anisotropic rotational motion of the cluster. The results are compared with corresponding data from cytochrome P-450 in microsomal form.

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