title: Caldesmon, acidic amino acids and molecular weight determinations.
abstract: Recent estimates of molecular weight and cDNA sequencing indicate that smooth muscle caldesmons are considerably smaller than previously thought. The anomalous behaviour of these proteins during SDS-polyacrylamide gel electrophoresis can be correlated with their high acidic amino acid content. The results suggest a need to re-evaluate the stoichiometric relations of caldesmon to tropomyosin and actin in thin filaments and its presumed 1:1 interaction with calmodulin.
authors.affiliation: Baylor College of Medicine, Houston, Texas 77030.
authors.forename: J
authors.initials: J
authors.lastname: Bryan
mesh_terms: D000596:Amino Acids / Q000032:analysis*; D002148:Calmodulin-Binding Proteins / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006801:Humans; D008970:Molecular Weight; D009130:Muscle, Smooth / Q000032:analysis*
chemical_list: D000596:Amino Acids; D002148:Calmodulin-Binding Proteins