1975/08/01 by John H. Collins, Marshall Elzinga · 217 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Biotin and Related Studies #thermodynamics and calorimetric analyses #Viral Infectious Diseases and Gene Expression in Insects #Cyanogen bromide #Protein primary structure #Peptide sequence #Peptide #Chemistry #Sequence (biology) #Cleavage (geology) #Tetrapeptide #Actin #Amino acid #Biochemistry #Stereochemistry #Biology
paper · doi:10.1016/s0021-9258(19)41139-3
published in Journal of Biological Chemistry 250(15), 5915-5920 (Elsevier BV)
openalex publication_date 1975/08/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/23
Actin is the principal constituent of the thin filaments of muscle, and in order to provide information basic to understanding the molecular basis of actin function we have studied its amino acid sequence. The isolation, compositions, and sequences of cyanogen bromide peptides, ranging in size from 3 to 44 residues, have previously been reported (ELZINGA, M. (1971) Biochemistry 10, 224-229, and other papers in the present series). The peptides have been aligned by isolation and characterization of tryptic peptides that contain methionine. The isolation of one of the CNBr peptides (CB-14) was complicated by the presence of a Met-Thr bond that was only partially split under standard conditions for cyanogen bromide cleavage in formic acid. In this paper conditions are described for increasing the cleavage at this bond. CB-14 is a tetrapeptide, Thr-Gln-Ile-Hse, and this sequence completes the characterization of the actin cyanogen bromide peptides. Finally, the position of CB-14 in the actin sequence as residues 120 to 123 was established by isolation of a chymotryptic overlap peptide. The complete sequence of the 374 residues of actin is presented.