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. 1975 May;147(2):221–228. doi: 10.1042/bj1470221

The actin content of fibroblasts.

D Bray, C Thomas
PMCID: PMC1165434  PMID: 1180890

Abstract

Cultures of chick skin fibroblasts were dissolved in solutions of sodium dodecyl sulphate, and their entire protein content was examined by gel electrophoresis. The most abundant species migrated in the same position as muscle actin. It gave a similar pattern of iodinated peptides after reaction with radioactive sodium iodide and digestion with proteinases, and contained comparable amounts of Nt-methylhistidine. Its amount was estimated by quantitative densitometry of stained gels with bovine serum albumin as an internal standard, and by radioactive assay of cultures that had been grown in the presence of [35S]methionine. The values obtained ranged from 7 to 14% of the total cellular protein, with an average of 8.5%. A protein band in the position of muscle myosin was also present and accounted for about 2.5% of the total protein. Both this and the actin band increased in relative amount with the age of the cultures.

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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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