Studies on the maintenance of cytochromes P-450 and b5, monooxygenases and cytochrome reductases in primary cultures of rat hepatocytes.

Abstract:

:The cytochrome P-450 content of rat hepatocytes declined rapidly over 72 h in culture, due primarily to denaturation to cytochrome P-420. Six different media were investigated for their ability to conserve cytochrome P-450 during culture, and the most successful was a modified Earle's medium. After 72 h culture in this medium, cytochromes P-450 and b5, NADH-cytochrome b5- and NADPH-cytochrome c-reductases were maintained at 40, 100, 35 and 52% of fresh cell values, respectively. Cytochrome P-450 showed differential functional stability during culture with ethoxyresorufin O-deethylation being more stable than either pentoxyphenoxazone O-depentylation or biphenyl 4-hydroxylation. Monooxygenase than did cytochrome P-450 content. This discrepancy was not explained by loss of flavin nucleotides, FMN or FAD.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Grant MH,Melvin MA,Shaw P,Melvin WT,Burke MD

doi

10.1016/0014-5793(85)80436-1

subject

Has Abstract

pub_date

1985-10-07 00:00:00

pages

99-103

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(85)80436-1

journal_volume

190

pub_type

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