[Solubilization of cerebral binding sites of S-adenosyl-L-homocysteine]

We describe the solubilization of S-adenosyl-L-homocysteine binding sites from rat brain membranes; Triton X100 could solubilize near 50% of the sites. The solubilized extract exhibited the same pH dependence as the membrane extract and had the same dissociation constant and the same sensibility to S-adenosyl-L-methionine and adenosine. The solubilized extract exhibited a methylase activity which accepted phosphatidylethanolamine as substrate.