Abstract
Actin preparations from striated muscle of beef, pig, lamb, chicken, frog, fish and pecten were compared with respect to their sedimentation coefficients, starch-gel electrophoresis, amino acid composition and peptide maps. No differences were found in the actin preparations from mammalian and avian muscle. When compared to mammalian actin, chemical differences were noted in the case of frog, fish and pecte actin. Actin from frog muscle differed only in the peptide map while the fish actin differed in amino acid composition and peptide map. The most pronounced differences appeard in the pecten actin which differed in starch-gel electrophoresis pattern, amino acid composition and peptide map. The results thus demonstrate structural differences between actins from species over a wide range of the evolutionary scale; the differences decreased with closer relationship of the specied.
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