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. 2001 Jul 23;154(2):435–446. doi: 10.1083/jcb.200105003

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Copyright © 2001, The Rockefeller University Press

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Figure 9. — Dystroglycan and α-latrotoxin compete for the same binding site in neurexins. Ig–N1α-1 was loaded with α-dystroglycan by incubation with an excess of total rat brain homogenate (lane 1) and extensive washing to remove nonbound proteins. Beads containing Ig–N1α-1 with bound dystroglycan were incubated with buffer containing the indicated amounts of α-latrotoxin and then centrifuged to separate unbound proteins in the supernatant (S) from bound proteins in the pellet (P). Fractions were analysed by immunoblotting for α-dystroglycan (top) and α-latrotoxin (bottom). Note that α-latrotoxin quantitatively displaces bound α-dystroglycan. The slight difference in migration of α-dystroglycan on the SDS-gels between supernatant (S) and pellet (P) fractions may be due to differences in the buffer composition of the samples loaded or to preferential binding of a subset of glycosylated forms of dystroglycan by neurexin 1α.