1973/09/01 by Marshall Elzinga, John H. Collins, W. Michael Kuehl +1 · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · #Biotin and Related Studies #thermodynamics and calorimetric analyses #Advanced Proteomics Techniques and Applications #Cyanogen bromide #Peptide sequence #Protein primary structure #Actin #Biochemistry #Sequence (biology) #Complete sequence #Histidine #Skeletal muscle #Amino acid #Biology #Cleavage (geology) #Chemistry #Molecular biology #Anatomy #Gene #Genome
paper · doi:10.1073/pnas.70.9.2687
openalex publication_date 1973/09/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/22
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.