Complete Amino-Acid Sequence of Actin of Rabbit Skeletal Muscle

Marshall Elzinga(Boston Biomedical Research Institute), John H. Collins(Boston Biomedical Research Institute), W. Michael Kuehl(Lung Institute), Robert Adelstein(Lung Institute)
Proceedings of the National Academy of Sciences
September 1, 1973
Cited by 399Open Access
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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 N(r)-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.


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