Elzinga M, Collins J H, Kuehl W M, Adelstein R S
Proc Natl Acad Sci U S A. 1973 Sep;70(9):2687-91. doi: 10.1073/pnas.70.9.2687.
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.
已确定兔骨骼肌肌动蛋白的完整氨基酸序列。肌动蛋白多肽链由374个残基组成，包括一个异常氨基酸N（r）-甲基组氨酸残基，计算分子量为41785。通过分离用溴化氰裂解该蛋白质产生的肽段、测定这些肽段的序列并确定它们在分子中的顺序来确定肌动蛋白的序列。这项研究代表了首次完整测定肌原纤维蛋白的氨基酸序列。将该序列与从不同来源分离的肌动蛋白的肽段进行比较表明，肌动蛋白的序列高度保守。
