Purification and characterization of a second form of hepatic cytochrome P-448 from rats treated with a pure polychlorinated biphenyl isomer.
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Biomedical subjects
Publications and source records attributed to P Linko.
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Hexachlorobenzene (HCB) produced increases in ethoxyresorufin (ERR) O-deethylase, aryl hydrocarbon hydroxylase (AHH) and aminopyrine N-demethylase activities in rat liver phenobarbital which were intermediate between those produced by phenobarbital and 3,4-benzpyrene (BP), alpha-Naphthoflavone (ANF) selectivity inhibited ERR activity in BP and HCB-induced microsomes (94% and 88%). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of liver microsomes indicated that HCB did not produce a detectable increase in a polypeptide with electrophoretic properties similar to those of purified cytochrome P-448 (Mr = 56,000). However, HCB did induce a polypeptide with Mr = 53,000 corresponding to one of two polypeptide bands induced by BP. This polypeptide may represent a second form of cytochrome P-448. Purification of HCB to remove possible dibenzo-p-dioxin impurities did not alter the 'mixed-type' induction produced by HCB. In contrast to HCB, all other chlorinated benzenes tested resembled phenobarbital as inducers.
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