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Microsomal membrane subfractionation by a lectin affinity method
Author(s) -
Sehmi D.,
Williams L.G.,
Williams D.J.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80352-0
Subject(s) - concanavalin a , microsome , lectin , membrane , biochemistry , chemistry , cell fractionation , chromatography , enzyme , in vitro
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.