Elucidation of human skeletal muscle tropomyosin sequences revealed three alpha-types and two beta-components with specific amino acid residue differences.
The elucidation of human skeletal muscle tropomyosin sequences reveals heterogeneity that will facilitate analysis of tropomyosin in developmental and diseased states.
Abstract The amino acid sequences of the human skeletal muscle tropomyosins were elucidated. Of the three α‐types identified, the major fraction (identical to the single myocardial species) differed by 23 and 25 amino acid residues from the two minor α‐forms and by 42 residues from β‐tropomyosin. The two β‐components differed only by deletion of the C‐terminal residue in the minor fraction. These sequences will facilitate analysis of tropomyosin from developmental and diseased states.
Romero-Herrera et al. (1982) studied this question. Amino acid sequencing of human skeletal muscle tropomyosins was evaluated on Amino acid sequence differences among tropomyosin isoforms. Elucidation of human skeletal muscle tropomyosin sequences revealed three alpha-types and two beta-components with specific amino acid residue differences.