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Effect of modification of sheep lung cytochrome P450LgM2(2B) by ethylacetimidate in hydroxylation activity
Date
1998-11-01
Author
Adalı, Orhan
Metadata
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Cytochrome P450LgM2(2B) purified from sheep lung microsomes was treated chemically using ethylacetimidate at pH 8.5 for 2 hours at room temperature. Ethylacetimidate modification of essential lysine residues of lung P450LgM2 caused an inhibition of catalytic activity P450 towards substrate benzphetamine. Benzphetamine N-demethylase activity of the reconstituted system containing modified P450LgM2 and purified sheep lung NADPH-cytochrome P450 reductase was inhibited by 93%. This inhibition may be due to an impaired interaction of P450LgM2 and reductase via electrostatic farces.
Subject Keywords
Cytochrome P450LgM2(2B)
,
Sheep lung
,
Benzphetamine
,
Ethylacetimidate
URI
https://hdl.handle.net/11511/54679
Journal
BIOCHEMICAL ARCHIVES
Collections
Department of Biology, Article
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O. Adalı, “Effect of modification of sheep lung cytochrome P450LgM2(2B) by ethylacetimidate in hydroxylation activity,”
BIOCHEMICAL ARCHIVES
, pp. 241–246, 1998, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/54679.