Abstract
1-Alkyl-2-acetyl- sn-glycero-3-phosphocholine possesses both hypotensive and platelet-activating properties. Our data show that after removal of the acetyl group at the sn-2 position by an acetyl hydrolase, the product, 1-alkyl-2-lyso- sn-glycero-3-phosphocholine, can be cleaved by a microsomal tetrahydropteridine-dependent alkyl monooxygenase in the liver and spleen of rats. Results obtained for the tetrahydropteridine requirement, tissue distribution, responses to thermal inactivation and catalase, and substrate inhibition of the enzyme indicate that the ether linkage of 1-alkyl-2-lyso- sn-glycero-3-phosphocholine is hydrolyzed by a monooxygenase that appears to be identical to the one responsible for cleavage of the O-alkyl moiety of alkylglycerols.
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