A fusion protein of @entity35 liver @entity7772 with @entity1110 -cytochrome P450 reductase was expressed genetically in @entity375 microsomal membranes. This flavo-cytochrome is active in 6-hydroxylation of @entity69871 . Rotational diffusion of the fusion protein was examined by observing the flash-induced absorption anisotropy r(t) of the P450.CO complex. Theoretical analysis of r(t) was performed based on a "rotation-about-membrane normal" model. The absorption anisotropy decayed within 2 ms to a time-independent value r(3). Forty percent of the fusion protein rotated with a rotational relaxation time phi of 1.35 ms. Treatment with high salt increased the mobile population of the fusion protein to 62% with phi = 0.96 ms. The mobile population of the fusion protein is close to that of @entity7772 coexpressed with the P450 reductase and greater than that of @entity7772 alone [Iwase et al. (1991) Biochemistry 30, 8347-8351]. The large mobile population of the fusion protein provides evidence that @entity7772 is mobilized by forming associations with P450 reductase in microsomal membranes.

Dynamic mobility of genetically expressed fusion protein between cytochrome P4501A1 and @entity1110 -cytochrome P450 reductase in XXXX microsomes.

@entity7772 :: ('24296(Tax:10116)', 'Gene') :: ['CYP1A1'] @entity69871 :: ('MESH:D015049', 'Chemical') :: ['zoxazolamine'] @entity1110 :: ('MESH:D009249', 'Chemical') :: ['NADPH'] @entity35 :: ('10116', 'Species') :: ['rat'] @entity375 :: ('4932', 'Species') :: ['yeast']
@entity375 :: (4932,Species) :: ['yeast']
