We use immunoblotting, immunoprecipitation, and centrifugation in sucr
ose density gradients to show that the product of the erythrocyte beta
-spectrin gene in rat skeletal muscle (muscle beta-spectrin) is presen
t in two states, one associated with fodrin, and another that is not a
ssociated with any identifiable spectrin or fodrin subunit. Immunofluo
rescence studies indicate that a significant amount of beta-spectrin w
ithout alpha-fodrin is present in the myoplasm of some muscle fibers,
and, more strikingly, at distinct regions of the sarcolemma. These res
ults suggest that alpha-fodrin and muscle beta-spectrin associate in m
uscle in situ, but that some muscle beta-spectrin without a paired alp
ha-subunit forms distinct domains at the sarcolemma. (C) 1997 Wiley-Li
ss, Inc.