Monoclonal antibody-directed immunopurification and identification of cytochromes P-450.

Abstract:

:Several rat liver cytochromes P-450 have been substantially purified in a one-step immunoadsorption procedure using Sepharose-bound monoclonal antibodies (MAbs) to the major forms of rat liver cytochrome P-450 induced by 3-methylcholanthrene and phenobarbital (MC-P-450 and PB-P-450, respectively). When mixed with solubilized rat liver microsomes the immunoadsorbent based on the MAb to MC-P-450 binds two polypeptides of MW 56,000 and 57,000 while the immunoadsorbent made with the MAb to PB-P-450 absorbs a species of MW 54,000. These polypeptides are readily desorbed by 0.1 M glycine (pH 3.0). Isolation of MAb-specific cytochrome P-450 isozymes by this method has applications in numerous phases of cytochrome P-450 research.

authors

Friedman FK,Robinson RC,Park SS,Gelboin HV

doi

10.1016/s0006-291x(83)80221-6

subject

Has Abstract

pub_date

1983-11-15 00:00:00

pages

859-65

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)80221-6

journal_volume

116

pub_type

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