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. 1973 Sep;70(9):2687–2691. doi: 10.1073/pnas.70.9.2687

Complete Amino-Acid Sequence of Actin of Rabbit Skeletal Muscle

Marshall Elzinga *, John H Collins *, W Michael Kuehl †, Robert S Adelstein †
PMCID: PMC427084  PMID: 4517681

Abstract

The complete amino-acid sequence of actin of rabbit skeletal muscle was determined. The actin polypeptide chain is composed of 374 residues, including one residue of the unusual amino acid Nr-methyl histidine, and has a calculated molecular weight of 41,785. The sequence of actin was determined by isolating the peptides produced by cleavage of the protein with cyanogen bromide, determining the sequence of these peptides, and establishing their order within the molecule. This study represents the first complete determination of the aminoacid sequence of a myofibrillar protein. Comparison of this sequence with peptides from actins isolated from different sources indicates that the sequence of actin is highly conserved.

Keywords: cyanogen bromide cleavage, maleation, myofibrillar protein, Nr-methyl histidine

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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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