Open AccessDiscovery of sphingosine 1‐ O ‐methyltransferase in rat kidney and liver homogenates 1
Author(s) -
SACKET Santosh J,
IM Dongsoon
Publication year - 2008
Publication title -
acta pharmacologica sinica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.514
H-Index - 90
eISSN - 1745-7254
pISSN - 1671-4083
DOI - 10.1111/j.1745-7254.2008.00857.x
Subject(s) - sphingosine , cytosol , enzyme , kidney , biochemistry , methyltransferase , chemistry , membrane , enzyme assay , biology , methylation , endocrinology , receptor , gene
Aim: To characterize sphingosine methyltransferase in rat tissues. Methods: By using S ‐adenosyl‐ L ‐(methyl‐ 3 H) methionine, enzymatic activity was measured in the rat liver and kidney homogenates. Results: The optimum pH and reaction time for the enzyme assay were pH 7.8 and 1 h. ZnCl 2 inhibited the activity, but not MgCl 2 , CaCl 2 , CoCl 2 , or NiCl 2 . In the kidney homogenate, enzymatic activity was detectable in the cytosol and all membrane fractions from the plasma membrane and other organelles; however, in the liver homogenate, enzymatic activity was detectable in all membrane fractions, but not in the cytosol. We also tested the enzymatic activity with structurally‐modified sphingosine derivatives. Conclusion: We found sphingosine 1‐ O ‐methyltransferase activity in the rat liver and kidney homogenates.