Actin in the Brush-Border of Epithelial Cells of the Chicken Intestine

AUTOR(ES)

Tilney, Lewis G.

RESUMO

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.

Documentos Relacionados

• Transport of thiamine by brush-border membrane vesicles from rat small intestine.
• Mechanisms of zinc transport into pig small intestine brush-border membrane vesicles.
• Phosphate transport in brush-border membranes from control and rachitic pig kidney and small intestine.
• Jejunal brush-border folate hydrolase. A novel enzyme.
• The effect of fasting on the potential difference across the brush-border membrane of enterocytes in rat small intestine.