Actin in the brush-border of epithelial cells of the chicken intestine.
The major soluble protein of the isolated brush-border of the intestinal epithelium has a molecular weight and net charge indistinguishable from those of skeletal-muscle actin, as determined by polyacrylamide gel electrophoresis. Furthermore, this protein, isolated from acetone powders of the purified brush-border, undergoes a G to F transformation in the presence of Mg(++). The filaments have a substructure indistinguishable from muscle actin, as seen by the negative-staining technique, and bind heavy meromyosin with the arrowhead configuration characteristic of actin. The filaments in the microvilli of the intact bruch-border also bind heavy meromyosin. Thus, actin seems to be present in intestinal epithelial cells.
D000199:Actins / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D004589:Electrophoresis, Disc; D004847:Epithelial Cells; D004848:Epithelium / Q000032:analysis; D007422:Intestines / Q000032:analysis*; D008854:Microscopy, Electron; D008970:Molecular Weight; D009124:Muscle Proteins / Q000032:analysis*; D015879:Myosin Subfragments / Q000378:metabolism; D011485:Protein Binding
D000199:Actins; D009124:Muscle Proteins; D015879:Myosin Subfragments