These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Mouse liver microsomal cholesterol epoxide hydrolase: a specific inhibition of its activity by 5,6 alpha-Imino-5 alpha-cholestan-3 alpha-OL. Author: Watabe T, Komatsu T, Isobe M, Tsubaki A. Journal: Chem Biol Interact; 1983; 44(1-2):143-54. PubMed ID: 6406079. Abstract: A comparative study on mouse liver epoxide hydrolase activities has been done by using enzyme inhibitors in order to obtain evidence for the specificity of microsomal cholesterol epoxide hydrolase. 5,6 alpha-Imino-5 alpha-cholestan-3 beta-ol (IC) strongly inhibited the microsomal hydrolysis of cholesterol alpha-epoxide and the other delta 5-steroid alpha-epoxides (0.1 mM each) at concentrations less than 1 microM but affected neither microsomal nor cytosolic hydrolysis of any other epoxides of endogenous and exogenous compounds (0.1 mM each). On the other hand, 3,3,3-trichloropropene 1,2-oxide (TCPO) did not inhibited the microsomal hydrolysis of delta 5-steroid alpha-epoxides but strongly inhibited both microsomal and cytosolic hydrolysis of the other epoxides used. The only exceptions for the epoxy substrates that were not affected by both inhibitors were 5 alpha-cholest-2-ene alpha- and beta-epoxides. The inhibition by IC of the microsomal cholesterol alpha-epoxide hydrolysis was competitive, but no significant inhibition of the enzyme activity was observed by the typical microsomal xenobiotic substrates, hexadecene oxide and benzo[a]pyrene 4,5-oxide. These results strongly suggest that the microsomal enzyme hydrolyzing cholesterol alpha-epoxide differs from the microsomal hydrolase for epoxides of various xenobiotic olefins and arenes.[Abstract] [Full Text] [Related] [New Search]