Conference paper

Reconversion of Cytochrome P420 into P450 and Reactivation of Hydroxylases in Microsomal Membranes Reconstituted by Self-Assembly

A. I. Archakov ; Research Centre of the Second Moscow Medical Institute, Moscow, USSR
G. I. Bachmanova ; Research Centre of the Second Moscow Medical Institute, Moscow, USSR
I. P. Kanaeva ; Research Centre of the Second Moscow Medical Institute, Moscow, USSR

Abstract

Membrane vesicles formed by means of dialysis of microsomal
proteins and lipids, solubilized by cholate, contained an equal
quantity of cytochromes P420 and P450. Addition of albumin and
phosphatidylcholine aids reconversion of cytochrome P420 into cytochrome
P450. In the presence of albumin the reconstituted membranes
contained less lysophosphatidylcholine than those reconstituted
without it. Comparative analysis does not reveal· marked
differences in the phospholipid and protein composition or specific
activity and content of NAD(P)H-dependent redox carriers of original
and reconstituted membranes. In contrast to original membranes,
the reconstituted ones do not possess aniline hydroxylase
activity. The NADH-specific dimethylaniline demethylase activity
was higher than that of the original membranes. NADPH-dependent
demethylase of this substrate could be reconstituted to
50-800/o of its initial activity. The reconstituted membranes differ
from original membranes by their higher non-enzymatic lipid peroxidase
activity. Thus, it appears that dialysis in the presence of
albumin and phosphatidylcholine is the most effective mode of
microsomal membrane reconstitution.

Keywords

Hrčak ID:

196376

URI

https://hrcak.srce.hr/196376

Publication date:

30.3.1977.

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