Abstract
Antibodies to electrolectin, a lectin endogenous to embryonic skeletal muscle, were used to study the distribution of electrolectin during myogenesis in L6 cells and rat primary muscle cultures. Antibody binding is highest to mononucleated cells and is low to myotubes in both systems. Binding is much lower to fibroblasts in the primary cultures. Binding appears to be on the surface of these cells, although evidence is presented for there being binding on the inside of cells as well. When observed on myotubes, binding is generally associated with highly stained patches and in some instances is near regions where fusion may be occurring. In L6 cells, binding sites can be exposed by treating mononucleated cells with trypsin.