Actins from various types of muscle across different animal phyla share similar primary structures regarding the positions of cysteinyl residues.
Answers are grounded in this paper and cite their sources.
Hypothesis-generating for actin conservation; leaves open relevance to human cardiac isoforms and disease.
Pure actins were obtained from various animal muscles: Vertebrata (skeletal, smooth, and cardiac muscles), Prochordata (smooth muscle), Nematoda (obliquely striated muscle), and Mollusca (striated, smooth and obliquely striated muscles). These actins were all identical in apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. All actins treated with 2-nitro-5-thiocyanobenzoic acid yielded four major (about 33,000, 26,000, 24,000, and less than 10,000 daltons) and three minor (22,000, 17,000, and 10,000 daltons) bands in addition to intact actin on gel electrophoresis. The results suggest that all actins from various types of muscle have cysteinyl residues at similar positions on the primary structure.
No takes yet. Share an insight, caveat, or question.
Nakamura et al. (1979) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: