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. 1971 Oct;68(10):2611–2615. doi: 10.1073/pnas.68.10.2611

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

Lewis G Tilney 1, Mark Mooseker 1
PMCID: PMC389479  PMID: 4944636

Abstract

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.

Keywords: electron microscopy, gel electrophoresis, G to F transformation, heavy meromyosin binding

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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