The study demonstrates a method for quantifying actin using an N-terminal peptide, revealing significant differences in apparent actin content between chicken breast muscle and fibroblasts, which may indicate sequence variations.
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Actin quantification differs markedly by avian tissue; leaves open validation and extension to human cardiac protein assays.
The isolation and quantification of an 18-residue peptide from the N-terminal region of chicken actin was used to quantify the amount of actin in acetone-dried powders of chicken breast muscle and chicken-embryo fibroblasts. Either isotope dilution or double labelling can be used for peptide quantification. About 17% of the protein of chicken breast muscle was estimated to be actin. However, only 0.25% of the protein of chicken-embryo fibroblasts was determined to be actin by quantification of this peptide. The actin content of fibroblasts may be low or the amino acid sequences of muscle and fibroblast actin may differ in the N-terminal region. The methodology used can be extended to examine whether other regions of muscle actin sequence are present in fibroblasts or other cell types.
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Peter J. Anderson (1976) studied this question.
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