Microsomal membrane subfractionation by a lectin affinity method.

Concanavalin A-agarose treatment of rat liver post-mitochondrial supernatant removes a fraction rich in cholesterol and 5'-nucleotidase activity but low in glucose-6-phosphatase. At the same time, radiolabel associated with the cell surface is removed. We interpret these findings as evidence that concanavalin A binds to, and under these circumstances will remove, fragments of plasma membrane present in the microsomal fraction and believe that this may be of use in the gentle, and rapid subfractionation of microsomal membranes.