Blanck J, Behlke J, Jänig G R, Pfeil D, Ruckpaul K
Acta Biol Med Ger. 1979;38(1):11-21.
The aerobic NADPH reduction of cytochrome P-450LM has been investigated on microsomes, as well as on the solubilized enzyme system in the associated, disintegrated, and reconstituted state, respectively. P-450 exhibits biphasic reduction kinetics of about 70/30% phase distribution and rate constants differing 10-fold. The partial reactions are due to organizational asymmetries, the cytochrome being either incorporated into P-450/reductase associates (cluster) or localized outside (randomly distributed, homoassociated, weakly cluster-associated). Triton N-101 disintegrates the different associate structures, consequently followed by the disappearance of the rapid reaction phase. The enzyme system can be reconstituted; at microsomal stoichiometry the respective standard parameters are approached, depending on the composition and structural organization of the phospholipid. The reorganization without any membrane matrix is obviously thermodynamically determined.
分别在微粒体以及处于缔合、解体和重组状态的溶解酶系统上研究了细胞色素P - 450LM的需氧NADPH还原。P - 450呈现出约70/30%相分布的双相还原动力学，速率常数相差10倍。部分反应归因于组织不对称性，细胞色素要么并入P - 450/还原酶缔合体（簇），要么定位于外部（随机分布、同缔合、弱簇缔合）。Triton N - 101使不同的缔合结构解体，随后快速反应相消失。酶系统可以重组；在微粒体化学计量比下，根据磷脂的组成和结构组织接近各自的标准参数。没有任何膜基质的重组显然是由热力学决定的。
