Different muscle-specific forms of rabbit skeletal muscle alpha-actinin

Abstract

The structures and functions of the two alpha-actinin isoforms [R. Kobayashi et al. (1983) Eur. J. Biochem. 133, 607-611] isolated from rabbit longissimus dorsi and psoas muscles were compared. One-dimensional and two-dimensional electrophoretic analyses showed that the two alpha-actinins were different from each other in their subunit chain weights and isoelectric points. The Stokes' radius of the longissimus dorsi and psoas alpha-actinins was 7.4 nm and 7.0 nm, respectively. The amino acid analyses showed that, although the two alpha-actinins are similar in their amino acid compositions, longissimus dorsi alpha-actinin contains more aspartic acid and isoleucine than psoas alpha-actinin but fewer glycine and valine residues. Analysis of the soluble tryptic peptides by two-dimensional mapping revealed that the two alpha-actinins had major differences. These data suggested that the two isoforms are the products of at least two different genes. Despite these differences, both alpha-actinins share a number of common properties. Both alpha-actinins contain a 55-kDa peptide resistant to trypsin. The two proteins show no differences in actomyosin turbidity assays. ATPase assays and F-actin binding assays of alpha-actinin activity. Immunological examination indicates that the two alpha-actinins share antigenic determinants in common.