Abstract:
:The FAD-containing monooxygenase (FMO) has been purified from both mouse and pig liver microsomes by similar purification procedures. Characterization of the enzyme from these two sources has revealed significant differences in catalytic and immunological properties. The pH optimum of mouse FMO is slightly higher than that of pig FMO (9.2 vs. 8.7) and, while pig FMO is activated 2-fold by n-octylamine, mouse FMO is activated less than 20%. Compounds, including primary, secondary and tertiary amines, sulfides, sulfoxides, thiols, thioureas and mercaptoimidazoles were tested as substrates for both the mouse and pig liver FMO. Km- and Vmax-values were determined for substrates representative of each of these groups. In general, the mouse FMO had higher Km-values for all of the amines and disulfides tested. Mouse FMO had Km-values similar to those of pig FMO for sulfides, mercaptoimidazoles, thioureas, thiobenzamide and cysteamine. Vmax-values for mouse FMO with most substrates was approximately equal, indicating that as with pig FMO, breakdown of the hydroxyflavin is the rate limiting step in the reaction mechanism. Either NADPH or NADH will serve as an electron donor for FMO, however, NADPH is the preferred donor. Pig and mouse FMOs have similar affinity for NADPH (Km = 0.97 and 1.1 microM, respectively) and for NADH (Km = 48 and 73 microM, respectively). An antibody, prepared by immunizing rabbits with purified pig liver FMO, reacts with purified pig liver FMO but not with mouse liver FMO, indicating structural differences between these two enzymes. This antibody inhibited pig FMO activity up to 60%.
journal_name
Chem Biol Interactjournal_title
Chemico-biological interactionsauthors
Sabourin PJ,Hodgson Edoi
10.1016/0009-2797(84)90025-5subject
Has Abstractpub_date
1984-09-15 00:00:00pages
125-39issue
2eissn
0009-2797issn
1872-7786pii
0009-2797(84)90025-5journal_volume
51pub_type
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journal_title:Chemico-biological interactions
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doi:10.1016/j.cbi.2008.04.001
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
pub_type: 杂志文章,评审
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journal_title:Chemico-biological interactions
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更新日期:2009-05-15 00:00:00
abstract::Microsomal epoxide hydrase (EH) and 176 000 g supernatant fraction glutathione-S-transferase (GSH-S-T) activities were determined with styrene oxide as substrate in rat testes during postnatal development. The development of these enzymes was also followed in liver for comparison. Testes of 6-day-old rats had high GSH...
journal_title:Chemico-biological interactions
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更新日期:1978-09-01 00:00:00